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PEGS: the essential protein engineering summit May 4-8, 2020 • Boston, MA Program | Conference programs include protein and antibody engineering, cancer immunotherapy, oncology, and emerging therapeutics. PEGS Europe 2018 Nov 12-16 Lisbon Portugal
PepTalk January
20-24, 2020• San Diego, CA Program |
covers a wide spectrum of applied protein sciences with emphasis on upstream R&D
engineering to downstream biologics production. antibody display: de Kruif J,, Boel E, Logtenberg T. Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions. J Mol Biol. 1995 Apr 21;248 (1): 97-105, April 1995 . aptamer: Aptamers are short nucleic acid sequences capable of specific, high-affinity molecular binding. They are isolated via SELEX (Systematic Evolution of Ligands by Exponential Enrichment), an evolutionary process that involves iterative rounds of selection and amplification before sequencing and aptamer characterization. As aptamers are genetic in nature, bioinformatic approaches have been used to improve both aptamers and their selection. Kinghorn AB, Fraser LA, Liang S, Shiu SC-C, Tanner JA. Aptamer Bioinformatics. International Journal of Molecular Sciences. 2017;18(12):2516. doi:10.3390/ijms18122516. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5751119/ A synthetic, specially- designed oligonucleotide with the ability to recognize and bind a protein ligand molecule or molecules with high affinity and specificity. Narrower terms: photoaptamers, Functional genomics Protein technologies peptide aptamer; Genomic technologies SELEX, spielgemers bacteriophage: Many phage have proved useful in the study of molecular biology and as vectors for the transfer of genetic information between cells … lambda bacteriophage can also undergo a lytic cycle or can enter a lysogenic cycle, in which the page DNA is incorporated into that of the host, awaiting a signal that initiates events leading to replication of the virus and lysis of the host cell. Glick The workhorse of phage display is the M13 bacteriophage virus. Related terms: phage, phage display bacteriophage, biopanning, phage; Labels, signaling & detection Proteomics directed protein evolution bait: The basic format of the yeast-two hybrid system involves the creation of two hybrid molecules, one in which the "bait" protein is fused with a transcription factor, and one in which the "prey" protein is fused with a related transcription factor. If the bait and prey proteins indeed interact then the two factors fused to these two proteins are also brought into proximity with each other. As a result a specific signal is produced, indicating an interaction has taken place. carbohydrate chips: University scientists have described the first chip- based chemical strategy for rapidly screening carbohydrates for biologically useful activity. [Chemical method makes further investigation of carbohydrates possible, Univ. of Chicago Chronicle, 21 (3) April 11, 2002] http://chronicle.uchicago.edu/020411/biochip.shtml carbohydrate microarrays: Stu Borman, Chemical and Engineering News, Dec. 16, 2002 lists as highlights of 2002 http://pubs.acs.org/cen/coverstory/8050/8050chemhighlights5.html with references to the literature on polysaccharide and glycoconjugate microarrays, monosaccharide chips, natural and synthetic oligosaccharide arrays, and synthetic oligosaccharides in microtiter plate format. cDNA phage display: Display cloning: functional identification of natural product receptors using cDNA-phage display. Sche PP, McKenzie KM, White JD, Austin DJ. Chem Biol. 1999 Oct;6(10):707- 716 co-immunoprecipitation Used to determine protein- protein interactions. An antibody is used to precipitate a protein along with bound proteins. John Yates, “Mass spectrometry and the Age of the Proteome” Journal Mass Spectrometry 33: 16, 1998 combinatorial biology: the creation of a large number of compounds (usually proteins or peptides) through technologies such as phage display. Similar to combinatorial chemistry, compounds are produced by biosynthesis rather than organic chemistry. This process was developed independently by Richard A. Houghten and H. Mario Geysen in the 1980s. Combinatorial biology allows the generation and selection of the large number of ligands for high-throughput screening.[1][2] Combinatorial biology techniques generally begin with large numbers of peptides, which are generated and screened by physically linking a gene encoding a protein and a copy of said protein. This could involve the protein being fused to the M13 minor coat protein pIII, with the gene encoding this protein being held within the phage particle. Large libraries of phages with different proteins on their surfaces can then be screened through automated selection and amplification for a protein that binds tightly to a particular target.[3] Wikipedia accessed 2018 Nov 8 https://en.wikipedia.org/wiki/Combinatorial_biology Related term: phage display co-precipitation: Method to identify interacting proteins by using antibodies to bind to the protein if immunoprecipitated under non- denaturing using conditions … (allow any other proteins bound to the protein known to be involved in a process) to precipitate rather than be washed away. depletion: Method of sample preparation which removes high abundance proteins (not of interest) from the sample. Related term: low- abundance proteins. directed evolution: Directed Evolution-Based Drug Discovery DNA Encoded Libraries and Other Diversity Oriented Platforms APRIL 9-10, 2019 San Diego CA Directed evolution approaches for drug discovery use genetic strategies (DNA-encoded, RNA-encoded or phage-based) to create very large but specific libraries of molecules whose amplification is driven by the target of interest. The theory was established decades ago but recently applications in early stage drug discovery have become more widespread. A few drug candidates arising from directed evolution campaigns are now in clinical trials. A bottleneck however of these diversity-oriented strategies is figuring out which hits to focus on from the many hits that are produced by these approaches. https://www.drugdiscoverychemistry.com/Directed-Evolution
a method used in protein
engineering that
mimics the process of natural
selection to
evolve proteins or nucleic
acids toward
a user-defined goal.[1] It
consists of subjecting a gene to
iterative rounds of mutagenesis (creating a library of variants),
selection (expressing the variants and isolating members with the desired
function), and amplification (generating a template for the next round).
It can be performed in vivo (in living cells), or in vitro (free
in solution or microdroplet). Directed evolution is used both for protein
engineering as
an alternative to rationally designing modified proteins, as well as
studies of fundamental evolutionary
principles in
a controlled, laboratory environment. Wikipedia accessed 2018 Sept 3
https://en.wikipedia.org/wiki/Directed_evolution
Directed evolution is an iterative process scientists use to design biological molecules like enzymes. It requires inducing some randomness in the target enzyme within an organism like bacteria. The resulting mutated bacteria are screened to see which ones do the intended job the best. The winners are then cultured, and from their offspring, the best are selected, and then cultured, and so on. https://www.vox.com/science-and-health/2018/10/3/17931612/nobel-prize-2018-chemistry-directed-evolution-enzymes-antibodies
directed protein evolution:
Systematic approaches to directed
evolution of proteins have been documented since the 1970s. The ability to
recruit new protein functions arises from the considerable substrate
ambiguity of many proteins. The substrate ambiguity of a protein can be
interpreted as the evolutionary potential that allows a protein to acquire
new specificities through mutation or to regain function via mutations
that differ from the original protein sequence. All organisms have
evolutionarily exploited this substrate ambiguity. When exploited in a
laboratory under controlled mutagenesis and selection, it enables a
protein to “evolve” in desired directions. One of the most effective
strategies in directed protein evolution is to gradually accumulate
mutations, either sequentially or by recombination, while applying
selective pressure. This is typically achieved by the generation of
libraries of mutants followed by efficient screening of these libraries
for targeted functions and subsequent repetition of the process using
improved mutants from the previous screening. Here we review some of the
successful strategies in creating protein diversity Yuan L, Kurek I,
English J, Keenan R. Laboratory-Directed Protein Evolution. Microbiology
and Molecular Biology Reviews. 2005;69(3):373-392.
doi:10.1128/MMBR.69.3.373-392.2005.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1197809/
DNA shuffling: Genomic technologies Can be used to evolve proteins. gene shuffling: Genomic technologies Can be used to evolve proteins. glycoarrays: Carbohydrate arrays (glycoarrays) have recently emerged as a high-throughput tool for studying carbohydrate-binding proteins and carbohydrate-processing enzymes. A number of sophisticated array platforms that allow for qualitative and quantitative analysis of carbohydrate binding and modification on the array surface have been developed, including analysis by fluorescence spectroscopy, mass spectrometry and surface plasmon resonance spectroscopy. Glycoarrays--tools for determining protein-carbohydrate interactions and glycoenzyme specificity. Laurent N1, Voglmeir J, Flitsch SL. Chem Commun (Camb). 2008 Oct 7;(37):4400-12. doi: 10.1039/b806983m. Epub 2008 Aug 5. https://pubs.rsc.org/en/Content/ArticleLanding/CC/2008/B806699J#!divAbstract https://www.ncbi.nlm.nih.gov/pubmed/18802573 glycoprotein microarrays: We employ carbohydrate and glycoprotein microarrays to analyze glycan- dependent gp120- protein interactions. In concert with new linking chemistries and synthetic methods, the carbohydrate arrays combine the advantages of microarray technology with the flexibility and precision afforded by organic synthesis. With these microarrays, we individually and competitively determined the binding profiles of five gp120 binding proteins, established the carbohydrate structural requirements for these interactions, and identified a potential strategy for HIV vaccine development. EW Adams et. al., Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology; glycan- dependent gp120/ protein interactions, Chem Biol. 11(6): 875- 881, June 2004 Related terms: oligosaccharide chips; Glycosciences glossary intrabodies: Recent advances in antibody engineering have now allowed the genes encoding antibodies to be manipulated so that the antigen binding domain can be expressed intracellularly. The specific and high- affinity binding properties of antibodies, combined with their ability to be stably expressed in precise intracellular locations inside mammalian cells, has provided a powerful new family of molecules for gene therapy applications. These intracellular antibodies are termed 'intrabodies'. Wayne A. Marasco, "Intrabodies: turning the humoral immune system outside in for intracellular immunization" Gene Therapy 4 (1): 11- 15, Jan. 1997 Isotope Coded Infinity Tag ICAT: These tags provide the ability to both identify and quantify a broad range of proteins in a high- throughput mode. Using ICAT reagents, researchers can compare the expression levels of proteins from two samples, such as from normal and diseased cells. ICAT reagents comprise a protein reactive group, an affinity tag (biotin), and an isotopically labeled linker. Related term: protein profiling molecular evolution protein: Evolution of proteins is studied by comparing the sequences and structures of proteins from many organisms representing distinct evolutionary clades. If the sequences/structures of two proteins are similar indicating that the proteins diverged from a common origin, these proteins are called as homologous proteins. More specifically, homologous proteins that exist in two distinct species are called as orthologs. Whereas, homologous proteins encoded by the genome of a single species are called paralogs. Wikipedia accessed 2018 Nov 10 https://en.wikipedia.org/wiki/Molecular_evolution#Protein_evolution molecular protein evolution directed: Systematic approaches to directed evolution of proteins have been documented since the 1970s. The ability to recruit new protein functions arises from the considerable substrate ambiguity of many proteins. The substrate ambiguity of a protein can be interpreted as the evolutionary potential that allows a protein to acquire new specificities through mutation or to regain function via mutations that differ from the original protein sequence. All organisms have evolutionarily exploited this substrate ambiguity. When exploited in a laboratory under controlled mutagenesis and selection, it enables a protein to “evolve” in desired directions. One of the most effective strategies in directed protein evolution is to gradually accumulate mutations, either sequentially or by recombination, while applying selective pressure. This is typically achieved by the generation of libraries of mutants followed by efficient screening of these libraries for targeted functions and subsequent repetition of the process using improved mutants from the previous screening. Here we review some of the successful strategies in creating protein diversity Yuan L, Kurek I, English J, Keenan R. Laboratory-Directed Protein Evolution. Microbiology and Molecular Biology Reviews. 2005;69(3):373-392. doi:10.1128/MMBR.69.3.373-392.2005.https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1197809/
molecular motors:
Protein based machines that are involved in
or cause movement such as the rotary devices (flagellar motor and the F1
ATPase) or the devices whose movement is directed along cytoskeletal filaments
(myosin, kinesin and dynein motor families). MeSH, 1999 oligosaccharide microarrays: Studies on glycans are indispensable to define complex life systems and cell communities because all living organisms consist of diverse cells, which are covered with an abundance of heterogeneous carbohydrates. Although studies on glycans are extremely difficult because of the lack of basic technologies common to DNAs and proteins, a few new aspects of glycotechnologies have now become realized in the form of 'bio- chips', which include 'oligosaccharide arrays' or 'glyco- chips'. Recently, Fukui et al. developed oligosaccharide microarrays for glycomic analysis of extensive carbohydrate- binding proteins. How and why such glyco- engineering projects have been made in the contexts of both pure and applied sciences is described. J. Hirabayashi, Oligosaccharide microarrays for glycomics, Trends in Biotechnology 21 (4): 141-143, Apr. 2003 Related terms: glycochip, glycoprotein arrays peptide aptamers: Engineered protein molecules selected from combinatorial libraries, [used] to dissect the function of specific genes and alleles, and to trace genetic pathways. Roger Brent "Peptide aptamers" Molecular Sciences Institute, 1999 Broader term: aptamers peptide arrays: Steve Fodor and colleagues at Affymax published several articles on these in the early 1990s. Related terms protein arrays, protein chips, protein microarrays Peptide Mass Fingerprinting PMF: A means of protein identification, using mass spectrometry peptide sequencing: How is this different from protein sequencing (except that peptides are shorter than proteins)? phage: A virus for which the natural host is a bacterial cell. DOE Used as a vector for cloning segments of DNA. Schlindwein Related terms: bacteriophage, phage display.
prefractionation: Sample preparation method, capable of being automated. protein arrays: Protein arrays are poised to become a central proteomics technology allowing for the global observation of biochemical activities on an unprecedented scale. Hundreds or thousands of proteins can be simultaneously screened for protein-protein, protein-nucleic acid, and small molecule interactions. The value of multiplexed protein measurement is being established in applications including: comprehensive proteomic surveys, studies of protein networks and pathways, validation of genomic discoveries, and clinical biomarker development. This technology holds great potential for basic molecular biology research, serum profiling, protein abundance determination, disease biomarker identification, immune and toxicological response profiling, and pharmaceutical target screening. Related terms: antibody arrays, protein chips, protein microarrays Narrower terms: high- density protein arrays, protein- protein interaction chips, proteome chip
protein capture
reagents:
The Common Fund’s Protein Capture Reagents
program is developing new resources and tools to understand the critical role
the multitude of cellular proteins play in normal development and health as well
as in disease. These resources will support a wide-range of research and
clinical applications that will enable the isolation and tracking of proteins of
interest and permit their use as diagnostic biomarkers of disease onset and
progression. NIH Common Fund http://commonfund.nih.gov/proteincapture/ Ciphergen trademarked ProteinChip™ which is now owned by BioRad. Some chips can operate with both nucleic acids and proteins. Analogous to DNA chips, these are used for studying protein expression or protein- protein interactions. Related terms: antibody arrays, carbohydrate chips, carbohydrate arrays, protein arrays, protein microarrays; Narrower terms: high- density protein microarrays, protein-protein interaction chips, proteome chip protein engineering: A technique used to produce proteins with altered or novel amino acid sequences. The methods used are: 1. Transcription and translation systems from synthesized lengths of DNA or RNA with novel sequences. 2. Chemical modification of 'normal' proteins. 3. Solid- state polypeptide synthesis to form proteins. IUPAC Compendium Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes. MeSH 2003
the process of
developing useful or valuable proteins. It is a young discipline, with
much research taking place into the understanding of protein
folding and recognition for protein
design principles. It is also a product and services market, with an
estimated value of $168 billion by 2017.[1] PEGS: the essential protein engineering summit May 4-5, 2020 • Boston, MA Program | protein inhibition: An alternative approach to [gene expression] downregulation, but in this case, the protein, not the gene, is the target. As with downregulation of gene expression, protein inhibition is a powerful target validation tool. The major approach to protein inhibition is based on phage libraries, which are used to select antibodies against targets of interest. protein knockouts: deGradFP (degrade Green Fluorescent Protein), an easy-to-implement protein knockout method applicable in any eukaryotic genetic system. Depleting a protein in order to study its function in a living organism is usually achieved at the gene level (genetic mutations) or at the RNA level (RNA interference and morpholinos). However, any system that acts upstream of the proteic level depends on the turnover rate of the existing target protein, which can be extremely slow. In contrast, deGradFP is a fast method that directly depletes GFP fusion proteins. In particular, deGradFP is able to counteract maternal effects in embryos and causes early and fast onset loss-of-function phenotypes of maternally contributed proteins. Protein Knockouts in Living Eukaryotes Using deGradFP and Green Fluorescent Protein Fusion Targets DOI: 10.1002/0471140864.ps3002s7 https://www.ncbi.nlm.nih.gov/pubmed/24510595 protein localization: There is an ever- increasing number of genes that have been sequenced but are of completely unknown function. The ability to determine the location of such gene products within the cell, either by the use of antibodies or by the production of chimeras with green fluorescent protein, is a vital step towards understanding what they do. This is one major reason why fluorescence microscopy is enjoying a revival. Protein Localization by Fluorescence Microscopy: A Practical Approach Edited by VICTORIA J. ALLAN, Oxford University Press, 2000 Narrower terms: subcellular localization, tissue specific localization; Related terms Cell biology: subcellular fractionation; Gene definitions: gene localization; Omes & omics localizome protein microarrays:
These arrays can consist of proteins themselves
(e.g., for studies of protein/ protein interactions or protein/ small- molecule
binding) or of probes for capturing proteins (so that protein levels in a sample
can be gauged).
Protein
microarrays will permit researchers to scan thousands of proteins in a variety
of proteomic experiments, including differential expression, response to drugs,
protein- protein interactions and identification of disease biomarkers. So far,
they have proven to be very quantitative and, by virtue of their addressable
arrays, much easier to compare results between experiments than 2D gels.
Commercialization of protein arrays also promises rapid development toward real
applications in clinical and point- of- care diagnostics, which would be
impossible with more complex proteomic technologies that require
electrophoresis
or chromatography. One disadvantage of the microarray approach is that generally
it is a "closed" system - you can only measure proteins for which you
have a capturing agent (such as an antibody).
Related
terms: antibody microarrays, protein arrays, protein chips, protein profiling
chips; Narrower terms: electrospray-
fabricated protein microarrays, functional protein microarrays, protein-protein
interaction chips, proteome chip protein purification: John Wagner's Logic of Molecular Approaches to Biological Problems (Cornell Univ. Graduate School of Medical Science, US ) has a section on the value of protein purification. http://www-users.med.cornell.edu/~jawagne/proteins_%26_purification.html proteolysis: Wikipedia http://en.wikipedia.org/wiki/Proteolysis Research and diagnostic applications proteolytic processing: Related terms proteolysis Broader term post- translational modification proteomics technologies: Major types include protein separation, ultrafiltration, 1D and 2D gel electrophoresis, liquid chromatography, capillary electrophoresis, mass spectrometry, protein informatics,protein arrays, protein quantification, protein localization, and protein- protein interactions. The application of proteomics technologies to clinical research and public health in general is an immediate goal of proteomics. A distantly related goal is the eventual application of proteomics to environmental, agricultural and veterinary research, research areas that are far less developed than clinical applications. Defining the Mandate of Proteomics in the Post- Genomics Era, Board on International Scientific Organizations, National Academy of Sciences, 2002 http://www.nap.edu/books/NI000479/html/R1.html For a field so laden with razzmatazz methods, it is striking that the number one need in proteomics may be new technology. There are simply not enough assays that are sufficiently streamlined to allow the automation necessary to perform them on a genome's worth of proteins. Those currently available barely scratch the surface of the thousands of specialized analyses biologists use every day on their favorite proteins. What we need are experimental strategies that could be termed cell biological genomics, biophysical genomics, physiological genomics, and so on, to provide clues to function. In addition, a protein contains so many types of information that each of its properties needs to be assayed on a proteome- wide scale, ideally in a quantitative manner. Stanley Fields "Proteomics in Genomeland" Science 291: 1221-1224 Feb. 16, 2001 self-assembling biomolecular materials: Examples of self- assembly include protein folding, the formation of liposomes, and the alignment of liquid crystals. While this type of equilibrium self- assembly is the central focus of this report, it is important to emphasize that much biological assembly is also driven by energy sources such as adenosine triphosphate (ATP), which power biomotors Biomolecular self- assembling materials, National Academy of Sciences 1996 http://www.nas.edu/bpa/reports/bmm/bmm.html#PBMM Broader term: self-assembly subcellular localization: A variety of approaches—including tagging and fluorescence technologies, cellular isolation methods, gels, and mass spectrometry—are being used in these studies, which aim to track the location and/or movement of proteins or protein complexes in subcellular compartments. translation: Sequences, DNA & beyond Another approach to downregulating gene expression See also Pharmaceutical biology antisense; RNA ribozymes. yeast display: (or yeast surface display): a protein engineering technique that uses the expression of recombinant proteins incorporated into the cell wall of yeast for isolating and engineering antibodies. Wikipedia accessed 2018 Oct 27 https://en.wikipedia.org/wiki/Yeast_display
Protein technologies resources IUPAC definitions are reprinted with the permission of the International Union of Pure and Applied Chemistry. |
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