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custom peptide synthesis


custom peptide synthesis

"Peptides" redirects here. For the journal, see Peptides (journal).

A tetrapeptide (example Val-Gly-Ser-Ala) with green marked amino end (L-Valine) and
blue marked carboxyl end (L-Alanine).
Peptides (from Greek language πεπτ??, peptós "digested"; derived from π?σσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.

The covalent chemical bonds are formed when the carboxyl group of one amino acid reacts with the amino group of another. The shortest peptides are dipeptides, consisting of 2 amino acids joined by a single peptide bond, followed by tripeptides, tetrapeptides, etc. A polypeptide is a long, continuous, and unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological oligomers and polymers, alongside nucleic acids, oligosaccharides and polysaccharides, etc.

Peptides are distinguished from proteins on the basis of size, and as an arbitrary benchmark can be understood to contain approximately 50 or fewer amino acids. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule (DNA, RNA, etc.), or to complex macromolecular assemblies. Finally, while aspects of the lab techniques applied to peptides versus polypeptides and proteins differ (e.g., the specifics of electrophoresis, chromatography, etc.), the size boundaries that distinguish peptides from polypeptides and proteins are not absolute: long peptides such as amyloid beta have been referred to as proteins, and smaller proteins like insulin have been considered peptides.

Amino acids that have been incorporated into peptides are termed "residues" due to the release of either a hydrogen ion from the amine end or a hydroxyl ion (OH?) from the carboxyl (COOH) end, or both, as a water molecule is released during formation of each amide bond. All peptides except cyclic peptides have an N-terminal and C-terminal residue at the end of the peptide (as shown for the tetrapeptide in the image).

custom peptide synthesis introduce Peptides Classes

Many kinds of peptides are known. They have been classified or categorized according to their sources and function. According to the Handbook of Biologically Active Peptides, some groups of peptides include plant peptides, bacterial/antibiotic peptides, fungal peptides, invertebrate peptides, amphibian/skin peptides, venom peptides, cancer/anticancer peptides, vaccine peptides , immune/inflammatory peptides, brain peptides, endocrine peptides, ingestive peptides, gastrointestinal peptides, cardiovascular peptides, renal peptides, respiratory peptides, opiate peptides, neurotrophic peptides, and blood–brain peptides.

Some ribosomal peptides are subject to proteolysis. These function, typically in higher organisms, as hormones and signaling molecules. Some organisms produce peptides as antibiotics, such as microcins.

Peptides frequently have posttranslational modifications such as phosphorylation, hydroxylation, sulfonation, palmitoylation, glycosylation and disulfide formation. In general, peptides are linear, although lariat structures have been observed. More exotic manipulations do occur, such as racemization of L-amino acids to D-amino acids in platypus venom.

Nonribosomal peptides are assembled by enzymes, not the ribosome. A common non-ribosomal peptide is glutathione, a component of the antioxidant defenses of most aerobic organisms. Other nonribosomal peptides are most common in unicellular organisms, plants, and fungi and are synthesized by modular enzyme complexes called nonribosomal peptide synthetases.

These complexes are often laid out in a similar fashion, and they can contain many different modules to perform a diverse set of chemical manipulations on the developing product. These peptides are often cyclic and can have highly complex cyclic structures, although linear nonribosomal peptides are also common. Since the system is closely related to the machinery for building fatty acids and polyketides, hybrid compounds are often found. The presence of oxazoles or thiazoles often indicates that the compound was synthesized in this fashion.

Peptide fragments refer to fragments of proteins that are used to identify or quantify the source protein. Often these are the products of enzymatic degradation performed in the laboratory on a controlled sample, but can also be forensic or paleontological samples that have been degraded by natural effects.

custom peptide synthesis introduce Peptides Uses in molecular biology

Use of peptides received prominence in molecular biology for several reasons. The first is that peptides allow the creation of peptide antibodies in animals without the need of purifying the protein of interest. This involves synthesizing antigenic peptides of sections of the protein of interest. These will then be used to make antibodies in a rabbit or mouse against the protein.

Another reason is that techniques such as mass spectrometry enable the identification of proteins based on the peptide masses and sequence that result from their fragmentation.

Peptides have recently been used in the study of protein structure and function. For example, synthetic peptides can be used as probes to see where protein-peptide interactions occur- see the page on Protein tags.

Inhibitory peptides are also used in clinical research to examine the effects of peptides on the inhibition of cancer proteins and other diseases. For example, one of the most promising application is through peptides that target LHRH. These particular peptides act as an agonist, meaning that they bind to a cell in a way that regulates LHRH receptors. The process of inhibiting the cell receptors suggests that peptides could be beneficial in treating prostate cancer. However, additional investigations and experiments are required before the cancer-fighting attributes, exhibited by peptides, can be considered definitive.

custom peptide synthesis introduce Peptides Number of amino acids

Peptides of defined length are named using IUPAC numerical multiplier prefixes.

A monopeptide has one amino acid.
A dipeptide has two amino acids.
A tripeptide has three amino acids.
A tetrapeptide has four amino acids.
A pentapeptide has five amino acids.
A hexapeptide has six amino acids.
A heptapeptide has seven amino acids.
An octapeptide has eight amino acids (e.g., angiotensin II).
A nonapeptide has nine amino acids (e.g., oxytocin).
A decapeptide has ten amino acids (e.g., gonadotropin-releasing hormone & angiotensin I).
A neuropeptide is a peptide that is active in association with neural tissue.
A lipopeptide is a peptide that has a lipid connected to it, and pepducins are lipopeptides that interact with GPCRs.
A peptide hormone is a peptide that acts as a hormone.
A proteose is a mixture of peptides produced by the hydrolysis of proteins. The term is somewhat archaic.
A peptidergic agent (or drug) is a chemical which functions to directly modulate the peptide systems in the body or brain. An example is opioidergics, which are neuropeptidergics.
Doping in sports
The term peptide has been used to mean secretagogue peptides and peptide hormones in sports doping matters: secretagogue peptides are classified as Schedule 2 (S2) prohibited substances on the World Anti-Doping Agency (WADA) Prohibited List, and are therefore prohibited for use by professional athletes both in and out of competition. Such secretagogue peptides have been on the WADA prohibited substances list since at least 2008. The Australian Crime Commission cited the alleged misuse of secretagogue peptides in Australian sport including growth hormone releasing peptides CJC-1295, GHRP-6, and GHSR (gene) hexarelin. There is ongoing controversy on the legality of using secretagogue peptides in sports.

custom peptide synthesis introduce See also

Beefy meaty peptide
CLE peptide
Epidermal growth factor
Journal of Peptide Science
Multifunctional peptides
Palmitoyl pentapeptide-4
Pancreatic hormone
Peptide Spectral Library
Peptide synthesis
Peptidomimetics (such as peptoids and β-peptides) to peptides, but with different properties.
Protein tag, describing addition of peptide sequences to enable protein isolation or detection



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A faster solid phase custom peptide synthesis method using ultrasonic agitation
Sonication accelerates couplings in the solid phase custom peptide synthesis.
Sonical custom peptide synthesis gives products with a higher purity than the classical approach.
Sonication does not cause the racemization of sensible residues (Cys, His).
The ultrasonic bath allows the parallel synthesis of many peptides.
Solid phase-supported synthesis is a widely used strategy in peptide chemistry. A factor which limits the product purity is the individual stages yields. Here, we reported that 
the use of ultrasonic agitation allows to reduce tenfold the time of synthesis in the Fmoc strategy and improve the purity of the final product. Our method is a promising 
alternative to traditional synthetic methods and microwave synthesizers.
Functionalized silica shell magnetic nanoparticles for nanophase custom peptide synthesis applications
New Nanostructured Support Synthesis for peptide preparation based on core–shell magnetic nanoparticles- silica was synthesized.
Different mesoporous structures of silica shell were explored to improve solvent dispersability and magnetic separation of nanoparticles.
Preliminary successful attempts of custom peptide synthesis involving several amino acids to assess the impact of steric hindrance were performed.
A new nanostructured solid phase synthesis magnetic support consisting of core-shell type magnetic nanoparticles based on magnetite, para-aminobenzoic acid (PABA) and secondary 
silica shell were synthesized by coprecipitation method and characterized. An newly designed organic linker with an ending hydroxyl group inspired by HMBA linker (4-hydroxy 
methyl benzamide) widely employed in classical peptide solid phase synthesis was obtained from 1,4-dimethylolbenzene and gamma-isocyanatopropyltriethoxysilane and was grafted on 
the surface in order to be used for the nanophase synthesis of peptides. Three reaction stages, yielding a tripeptide sequence, using n-terminal protected amino acids and the 
principle of solid phase synthesis through the Fmoc strategy were performed, in order to prove the effectiveness of the nanophase custom peptide synthesis. The MS analysis 
confirmed the success of the tricustom peptide synthesis, recommending the new nanostructured system as a solid support in the solid phase synthesis of peptides. The 
intermediate and final materials were analysed by advanced characterization methods (SEM, TEM, BET, X-ray diffraction, magnetic properties, DLS, FT-IR, NMR for organic 
intermediates characterization, TGA and LC-MS).
Effect of high hydrostatic pressure on prebiotic custom peptide synthesis
Prebiotic custom peptide synthesis is a central issue concerning life’s origins. Many studies considered that life might come from Hadean deep-sea environment, that is, under 
high hydrostatic pressure conditions. However, the properties of prebiotic peptide formation under high hydrostatic pressure conditions have seldom been mentioned. Here we 
report that the yields of dipeptides increase with raised pressures. Significantly, effect of pressure on the formation of dipeptide was obvious at relatively low temperature. 
Considering that the deep sea is of high hydrostatic pressure, the pressure may serve as one of the key factors in prebiotic custom peptide synthesis in the Hadean deep-sea 
environment. The high hydrostatic pressure should be considered as one of the significant factors in studying the origin of life.
Graphical abstract
Here we report that the high hydrostatic pressure, as a key factor of deep-sea environment conditions, promoted the peptide formation and should be considered as one of the 
significant factors in studying the origin of life.
Bicyclic peptides: types, synthesis and applications
Bicyclic peptides categorized into two groups: natural and synthetic.
Bicyclic peptides form one of the promising platforms for drug development owing to their biocompatibility, similarity and chemical diversity to proteins.
Bicyclic peptides can be employed as effective alternatives to complex molecules, such as antibodies, or small chemical molecules.
Bicyclic peptides can be used as antimicrobial agents, drug targeting, imaging and diagnosis agents and therapeutics tools.
Bicyclic peptides form one of the most promising platforms for drug development owing to their biocompatibility, similarity and chemical diversity to proteins, and they are 
considered as a possible practical tool in various therapeutic and diagnostic applications. Bicyclic peptides are known to have the capability of being employed as an effective 
alternative to complex molecules, such as antibodies, or small molecules. This review provides a summary of the recent progress on the types, synthesis and applications of 
bicyclic peptides. More specifically, natural and synthetic bicyclic peptides are introduced with their different production methods and relevant applications, including drug 
targeting, imaging and diagnosis. Their uses as antimicrobial agents, as well as the therapeutic functions of different bicyclic peptides, are also discussed.
Antimicrobial alumina nanobiostructures of disulfide- and triazole-linked peptides: Synthesis, characterization, membrane interactions and biological activity
Synthesis and characterization of a new disulfide and triazole-peptide-decorated alumina nanoparticles.
Relevant biological activity of hybrid nanobiostructures containing antimicrobial peptides.
Membrane-interactions of the new synthesized nanobiostructures.
Due to the its physical-chemical properties, alumina nanoparticles have potential applications in several areas, such as nanobiomaterials for medicinal or orthodontic implants, 
although the introduction of these devices poses a serious risk of microbial infection. One convenient strategy to circumvent this problem is to associate the nanomaterials to 
antimicrobial peptides with broad-spectrum of activities. In this study we present two novel synthesis approaches to obtain fibrous type alumina nanoparticles covalently bound 
to antimicrobial peptides. In the first strategy, thiol functionalized alumina nanoparticles were linked via disulfide bond formation to a cysteine residue of an analog of the 
peptide BP100 containing a four amino acid spacer (Cys-Ala-Ala-Ala). In the second strategy, alumina nanoparticles were functionalized with azide groups and then bound to 
alkyne-decorated analogs of the peptides BP100 and DD K through a triazole linkage obtained via a copper(I)-catalyzed cycloaddition reaction. The complete physical-chemical 
characterization of the intermediates and final materials is presented along with in vitro biological assays and membrane interaction studies, which confirmed the activity of 
the obtained nanobiostructures against both bacteria and fungi. To our knowledge, this is the first report of aluminum nanoparticles covalently bound to triazole-peptides and to 
a disulfide bound antimicrobial peptide with high potential for biotechnological applications.
Iterative custom peptide synthesis in membrane cascades: Untangling operational decisions
Dynamic process model of semi-batch custom peptide synthesis in membrane cascade was developed.
Model validation by experimental data.
Reactions, side-reactions and diafiltration included in the process model.
Further study by readers is enabled by the downloadable simulation file (gPROMS).
Membrane enhanced custom peptide synthesis (MEPS) combines liquid-phase synthesis with membrane filtration, avoiding time-consuming separation steps such as precipitation and 
drying. Although performing MEPS in a multi-stage cascade is advantageous over a single-stage configuration in terms of overall yield, this is offset by the complex combination 
of operational variables such as the diavolume and recycle ratio in each diafiltration process. This research aims to tackle this problem using dynamic process simulation. The 
results suggest that the two-stage membrane cascade improves the overall yield of MEPS significantly from 72.2% to 95.3%, although more washing is required to remove impurities 
as the second-stage membrane retains impurities together with the anchored peptide. This clearly indicates a link between process configuration and operation. While the case 
study is based on the comparison of single-stage and two-stage MEPS, the results are transferable to other biopolymers such as oligonucleotides, and more complex system 
configurations (e.g. three-stage MEPS).

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