View source for Peptide

{{Short description|Short chains of 2–50 amino acids}}
{{Redirect|Peptides|the journal|Peptides (journal)}}
[[File:Drosomycin.svg|thumb|[[Drosomycin]], an example of a peptide]]

'''Peptides''' are short chains of [[amino acid]]s linked by [[peptide bond]]s.<ref>{{Cite book |last=Hamley |first=I. W. |url=https://www.wiley.com/en-ai/Introduction+to+Peptide+Science-p-9781119698173 |title=introduction to Peptide Science |date=September 2020 |publisher=Wiley |isbn=978-1-119-69817-3}}</ref><ref>{{Lehninger4th}}</ref> A '''polypeptide''' is a longer, continuous, unbranched peptide chain.<ref name="Saladin">{{Cite book |last=Saladin |first=K. |title=Anatomy & physiology: the unity of form and function |date=13 January 2011 |publisher=McGraw-Hill |isbn=978-0-07-337825-1 |edition=6th |page=67}}</ref> Polypeptides that have a [[molecular mass]] of 10,000 [[Dalton (unit)|Da]] or more are called [[protein]]s.<ref>{{GoldBookRef |title=proteins |file=P04898}}.</ref> Chains of fewer than twenty amino acids are called [[oligopeptide]]s, and include [[dipeptide]]s, [[tripeptide]]s, and [[tetrapeptide]]s.

Peptides fall under the broad chemical classes of [[biopolymer|biological polymers]] and [[oligomer]]s, alongside [[nucleic acid]]s, [[oligosaccharide]]s, [[polysaccharide]]s, and others.

Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to [[ligand (biochemistry)|ligand]]s such as [[coenzyme]]s and [[cofactor (biochemistry)|cofactor]]s, to another protein or other [[macromolecule]] such as [[DNA]] or [[RNA]], or to complex [[macromolecular assemblies]].<ref>{{Cite journal |last1=Ardejani |first1=Maziar S. |last2=Orner |first2=Brendan P. |date=2013-05-03 |title=Obey the Peptide Assembly Rules |journal=Science |volume=340 |issue=6132 |pages=561–562 |bibcode=2013Sci...340..561A |doi=10.1126/science.1237708 |issn=0036-8075 |pmid=23641105 |s2cid=206548864}}</ref>

Amino acids that have been incorporated into peptides are termed [[Residue (chemistry)#Biochemistry|residues]]. A water molecule is released during formation of each [[amide]] bond.<ref name="IUPAC1">{{GoldBookRef|file=A00279|title=amino-acid residue in a polypeptide}}.</ref> All peptides except [[cyclic peptide]]s have an [[N-terminus|N-terminal]] (amine group) and [[C-terminus|C-terminal]] (carboxyl group) residue at the end of the peptide (as shown for the tetrapeptide in the image).

== Classification ==

Cells make insulin through two main steps: transcription and translation. First, in the nucleus of pancreatic β-cells, the insulin gene on the DNA is transcribed by RNA polymerase to produce a strand of mRNA, which carries the instructions for making insulin. This mRNA then moves into the cytoplasm and attaches to a ribosome, where translation occurs. During translation, the ribosome reads the mRNA codons and tRNA molecules bring the correct amino acids to build the initial protein called preproinsulin. This protein is then processed in the rough ER and Golgi apparatus, where it is trimmed and folded to form proinsulin, and finally converted into active insulin by removing the C-peptide. The finished insulin is stored in vesicles and released into the bloodstream when blood glucose levels rise.

Peptides frequently have [[post-translational modification]]s such as [[phosphorylation]], [[hydroxylation]], [[sulfonation]], [[palmitoylation]], glycosylation, and [[disulfide bridge|disulfide]] formation. In general, peptides are linear, although [[splicing (genetics)|lariat]] structures have been observed.<ref>{{Cite journal |vauthors=Pons M, Feliz M, Antònia Molins M, Giralt E |date=May 1991 |title=Conformational analysis of bacitracin A, a naturally occurring lariat |journal=Biopolymers |volume=31 |issue=6 |pages=605–12 |doi=10.1002/bip.360310604 |pmid=1932561 |s2cid=10924338}}</ref> More exotic manipulations do occur, such as racemization of L-amino acids to D-amino acids in [[platypus venom]].<ref>{{Cite journal |vauthors=Torres AM, Menz I, Alewood PF, etal |date=July 2002 |title=D-Amino acid residue in the C-type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus |journal=FEBS Letters |volume=524 |issue=1–3 |pages=172–6 |bibcode=2002FEBSL.524..172T |doi=10.1016/S0014-5793(02)03050-8 |pmid=12135762 |s2cid=3015474}}</ref>

''[[Nonribosomal peptide]]s'' are assembled by [[enzyme]]s, not the ribosome. A common non-ribosomal peptide is [[glutathione]], a component of the [[antioxidant]] defenses of most aerobic organisms.<ref name="MeisterB">{{Cite journal |last1=Meister A, Anderson ME |last2=Anderson |year=1983 |title=Glutathione |journal=Annual Review of Biochemistry |volume=52 |issue=1 |pages=711–60 |doi=10.1146/annurev.bi.52.070183.003431 |pmid=6137189}}</ref> Other nonribosomal peptides are most common in [[unicellular organism]]s, [[plant]]s, and [[fungi]] and are synthesized by [[Modularity (biology)|modular]] enzyme complexes called ''nonribosomal peptide synthetases''.<ref>{{Cite journal |last1=Hahn M, Stachelhaus T |last2=Stachelhaus |date=November 2004 |title=Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=101 |issue=44 |pages=15585–90 |bibcode=2004PNAS..10115585H |doi=10.1073/pnas.0404932101 |pmc=524835 |pmid=15498872 |doi-access=free}}</ref>

{{anchor|Peptone}}

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.<ref>{{Cite journal |last1=Finking R, Marahiel MA |last2=Marahiel |year=2004 |title=Biosynthesis of nonribosomal peptides1 |journal=Annual Review of Microbiology |volume=58 |issue=1 |pages=453–88 |doi=10.1146/annurev.micro.58.030603.123615 |pmid=15487945}}</ref> These peptides are often [[Cyclic compound|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 acid]]s and [[polyketide]]s, hybrid compounds are often found. The presence of [[oxazoles]] or [[thiazoles]] often indicates that the compound was synthesized in this fashion.<ref>{{Cite journal |last1=Du L, Shen B |last2=Shen |date=March 2001 |title=Biosynthesis of hybrid peptide-polyketide natural products |journal=Current Opinion in Drug Discovery & Development |volume=4 |issue=2 |pages=215–28 |pmid=11378961}}</ref>

Peptones are derived from animal milk or meat digested by [[proteolysis]].<ref>{{Cite web |title=UsvPeptides- USVPeptides is a leading pharmaceutical company in India |url=http://www.usvpeptides.com |website=USVPeptides}}</ref> In addition to containing small peptides, the resulting material includes fats, metals, salts, vitamins, and many other biological compounds. Peptones are used in nutrient media for growing bacteria and fungi.<ref>{{Cite book |last1=Payne |first1=J. W. |title=Advances in Microbial Physiology, Volume 13 |last2=Rose |first2=Anthony H. |last3=Tempest |first3=D. W. |date=27 September 1974 |publisher=Elsevier Science |isbn=978-0-08-057971-9 |volume=13 |location=Oxford, England |pages=55–160 |chapter=Peptides and micro-organisms |journal=Advances in Microbial Physiology |doi=10.1016/S0065-2911(08)60038-7 |oclc=1049559483 |pmid=775944 |chapter-url=https://books.google.com/books?id=QgQuTYSW8A4C&dq=peptides&pg=PA147}}</ref>

''Peptide fragments'' refer to fragments of proteins that are used to identify or quantify the source protein.<ref>{{Cite journal |vauthors=Hummel J, Niemann M, Wienkoop S, Schulze W, Steinhauser D, Selbig J, Walther D, Weckwerth W |year=2007 |title=ProMEX: a mass spectral reference database for proteins and protein phosphorylation sites |journal=BMC Bioinformatics |volume=8 |issue=1 |page=216 |doi=10.1186/1471-2105-8-216 |pmc=1920535 |pmid=17587460 |doi-access=free}}</ref> 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.<ref>{{Cite book |last1=Webster J, Oxley D |title=Chemical Genomics |last2=Oxley |year=2005 |isbn=978-1-58829-399-2 |series=Methods in Molecular Biology |volume=310 |pages=227–40 |chapter=Peptide Mass Fingerprinting |doi=10.1007/978-1-59259-948-6_16 |pmid=16350956 |chapter-url=https://archive.org/details/chemicalgenomics00zand_0/page/227 |chapter-url-access=registration}}</ref><ref>{{Cite journal |last1=Marquet P, Lachâtre G |last2=Lachâtre |date=October 1999 |title=Liquid chromatography-mass spectrometry: potential in forensic and clinical toxicology |journal=Journal of Chromatography B |volume=733 |issue=1–2 |pages=93–118 |doi=10.1016/S0378-4347(99)00147-4 |pmid=10572976}}</ref>

== Chemical synthesis ==
{{Main|Peptide synthesis}}
[[File:Peptide Synthesis.svg|thumb|centre|upright=3.0|alt=Table of amino acids| Solid-phase peptide synthesis on a rink amide [[resin]] using [[Fmoc]]-α-[[amine]]-protected [[amino acid]]]]

== Protein-peptide interactions ==
[[File:Protein-peptide interaction.png|thumb|Example of a protein (orange) and peptide (green) interaction. Obtained from Propedia: a peptide-protein interactions database.<ref>{{Cite web |title=Propedia v2.3 - Peptide-Protein Interactions Database |url=http://bioinfo.dcc.ufmg.br/propedia2/ |access-date=2023-03-28 |website=bioinfo.dcc.ufmg.br}}</ref>]]
Peptides can perform interactions with proteins and other macromolecules. They are responsible for numerous important functions in human cells, such as cell signaling, and act as immune modulators.<ref name=":0">{{Cite journal |last1=Martins |first1=Pedro M. |last2=Santos |first2=Lucianna H. |last3=Mariano |first3=Diego |last4=Queiroz |first4=Felippe C. |last5=Bastos |first5=Luana L. |last6=Gomes |first6=Isabela de S. |last7=Fischer |first7=Pedro H. C. |last8=Rocha |first8=Rafael E. O. |last9=Silveira |first9=Sabrina A. |last10=de Lima |first10=Leonardo H. F. |last11=de Magalhães |first11=Mariana T. Q. |last12=Oliveira |first12=Maria G. A. |last13=de Melo-Minardi |first13=Raquel C. |date=December 2021 |title=Propedia: a database for protein–peptide identification based on a hybrid clustering algorithm |journal=BMC Bioinformatics |language=en |volume=22 |issue=1 |page=1 |doi=10.1186/s12859-020-03881-z |issn=1471-2105 |pmc=7776311 |pmid=33388027 |doi-access=free}}</ref> Indeed, studies have reported that 15-40% of all protein-protein interactions in human cells are mediated by peptides.<ref>{{Cite journal |last1=Neduva |first1=Victor |last2=Linding |first2=Rune |last3=Su-Angrand |first3=Isabelle |last4=Stark |first4=Alexander |last5=Masi |first5=Federico de |last6=Gibson |first6=Toby J |last7=Lewis |first7=Joe |last8=Serrano |first8=Luis |last9=Russell |first9=Robert B |date=2005-11-15 |editor-last=Matthews |editor-first=Rowena |title=Systematic Discovery of New Recognition Peptides Mediating Protein Interaction Networks |journal=PLOS Biology |language=en |volume=3 |issue=12 |article-number=e405 |doi=10.1371/journal.pbio.0030405 |issn=1545-7885 |pmc=1283537 |pmid=16279839 |doi-access=free}}</ref> Additionally, it is estimated that at least 10% of the pharmaceutical market is based on peptide products.<ref name=":0" />

== Example families ==
The peptide families in this section are ribosomal peptides, usually with hormonal activity. All of these peptides are synthesized by cells as longer "[[propeptide]]s" or "proproteins" and truncated prior to exiting the cell. They are released into the bloodstream where they perform their signaling functions.<ref>{{Cite web |date=2025-01-11 |title=Protein Synthesis: From Ribosomes to Post-Translational Modifications |url=https://biologyinsights.com/protein-synthesis-from-ribosomes-to-post-translational-modifications/ |access-date=2025-04-04 |website=BiologyInsights |language=en-US}}</ref>

=== Antimicrobial peptides ===
* [[Magainin]] family
* [[Cecropin]] family
* [[Cathelicidin]] family
* [[Defensin]] family

=== Tachykinin peptides ===
{{main | Tachykinin peptides}}
* [[Substance P]]
* [[Kassinin]]
* [[Neurokinin A]]
* [[Eledoisin]]
* [[Neurokinin B]]

=== Vasoactive intestinal peptides ===
{{main | Secretin family}}
* [[Vasoactive intestinal peptide|VIP]] ('''''V'''asoactive '''I'''ntestinal '''P'''eptide''; PHM27)
* [[Pituitary adenylate cyclase activating peptide|PACAP]] '''''P'''ituitary '''A'''denylate '''C'''yclase '''A'''ctivating '''P'''eptide''
* [[Peptide PHI]] 27 ('''''P'''eptide '''H'''istidine '''I'''soleucine 27'')
* [[Growth hormone releasing hormone|GHRH]] 1-24 ''('''G'''rowth '''H'''ormone '''R'''eleasing '''H'''ormone 1-24)''
* [[Glucagon]]
* [[Secretin]]

=== Pancreatic polypeptide-related peptides ===
* [[Neuropeptide Y|NPY]] ''('''N'''euro'''P'''eptide '''Y''')
* [[Peptide YY|PYY]] ''('''P'''eptide '''YY''')''
* APP ''('''A'''vian '''P'''ancreatic '''P'''olypeptide)''
* [[Pancreatic polypeptide|PPY]] '''''P'''ancreatic '''P'''ol'''Y'''peptide''

=== Opioid peptides ===
{{main|Opioid peptide}}
* [[Proopiomelanocortin]] (POMC) peptides
* [[Enkephalin]] pentapeptides
* [[Prodynorphin]] peptides

=== Calcitonin peptides ===
* [[Calcitonin]]
* [[Amylin]]
* [[AGG01]]

=== Self-assembling peptides ===
* [[Aromatic short peptides]]<ref>{{Cite journal |last1=Tao |first1=Kai |last2=Makam |first2=Pandeeswar |last3=Aizen |first3=Ruth |last4=Gazit |first4=Ehud |date=17 Nov 2017 |title=Self-assembling peptide semiconductors |journal=Science |volume=358 |issue=6365 |article-number=eaam9756 |doi=10.1126/science.aam9756 |pmc=5712217 |pmid=29146781}}</ref><ref>{{Cite journal |last1=Tao |first1=Kai |last2=Levin |first2=Aviad |last3=Adler-Abramovich |first3=Lihi |last4=Gazit |first4=Ehud |date=26 Apr 2016 |title=Fmoc-modified amino acids and short peptides: simple bio-inspired building blocks for the fabrication of functional materials |journal=Chem. Soc. Rev. |volume=45 |issue=14 |pages=3935–3953 |doi=10.1039/C5CS00889A |pmid=27115033}}</ref>
* [[Biomimetic peptides]]<ref>{{Cite journal |last1=Tao |first1=Kai |last2=Wang |first2=Jiqian |last3=Zhou |first3=Peng |last4=Wang |first4=Chengdong |last5=Xu |first5=Hai |last6=Zhao |first6=Xiubo |last7=Lu |first7=Jian R. |date=February 10, 2011 |title=Self-Assembly of Short Aβ(16−22) Peptides: Effect of Terminal Capping and the Role of Electrostatic Interaction |journal=Langmuir |volume=27 |issue=6 |pages=2723–2730 |doi=10.1021/la1034273 |pmid=21309606}}</ref>
* [[Peptide amphiphile]]s<ref>{{Cite journal |last=Ian Hamley |date=2011 |title=Self-Assembly of Amphiphilic Peptides |url=http://centaur.reading.ac.uk/19780/1/AmphPeptReviewRevised.pdf |journal=Soft Matter |volume=7 |issue=9 |pages=4122–4138 |bibcode=2011SMat....7.4122H |doi=10.1039/C0SM01218A}}</ref><ref>{{Cite journal |last1=Kai Tao |last2=Guy Jacoby |last3=Luba Burlaka |last4=Roy Beck |last5=Ehud Gazit |date=July 26, 2016 |title=Design of Controllable Bio-Inspired Chiroptic Self-Assemblies |journal=Biomacromolecules |volume=17 |issue=9 |pages=2937–2945 |doi=10.1021/acs.biomac.6b00752 |pmid=27461453}}</ref><ref>{{Cite journal |last1=Kai Tao |last2=Aviad Levin |last3=Guy Jacoby |last4=Roy Beck |last5=Ehud Gazit |date=23 August 2016 |title=Entropic Phase Transitions with Stable Twisted Intermediates of Bio-Inspired Self-Assembly |journal=Chem. Eur. J. |volume=22 |issue=43 |pages=15237–15241 |doi=10.1002/chem.201603882 |pmid=27550381}}</ref><ref>{{Cite journal |last1=Donghui Jia |last2=Kai Tao |last3=Jiqian Wang |last4=Chengdong Wang |last5=Xiubo Zhao |last6=Mohammed Yaseen |last7=Hai Xu |last8=Guohe Que |last9=John R. P. Webster |last10=Jian R. Lu |date=June 16, 2011 |title=Dynamic Adsorption and Structure of Interfacial Bilayers Adsorbed from Lipopeptide Surfactants at the Hydrophilic Silicon/Water Interface: Effect of the Headgroup Length |journal=Langmuir |volume=27 |issue=14 |pages=8798–8809 |doi=10.1021/la105129m |pmid=21675796}}</ref>
* Peptide dendrimers<ref>{{Cite journal |last1=Heitz |first1=Marc |last2=Javor |first2=Sacha |last3=Darbre |first3=Tamis |last4=Reymond |first4=Jean-Louis |date=2019-08-21 |title=Stereoselective pH Responsive Peptide Dendrimers for siRNA Transfection |journal=Bioconjugate Chemistry |language=en |volume=30 |issue=8 |pages=2165–2182 |doi=10.1021/acs.bioconjchem.9b00403 |issn=1043-1802 |pmid=31398014 |s2cid=199519310}}</ref>

=== Other peptides ===
* [[Ventricular natriuretic peptide|B-type Natriuretic Peptide (BNP)]] – produced in the myocardium and useful in medical diagnosis
* [[Lactotripeptides]] – Lactotripeptides might reduce [[blood pressure]],<ref>{{Cite journal |last1=Boelsma E, Kloek J |last2=Kloek |date=March 2009 |title=Lactotripeptides and antihypertensive effects: a critical review |journal=The British Journal of Nutrition |volume=101 |issue=6 |pages=776–86 |doi=10.1017/S0007114508137722 |pmid=19061526 |doi-access=free}}</ref><ref>{{Cite journal |vauthors=Xu JY, Qin LQ, Wang PY, Li W, Chang C |date=October 2008 |title=Effect of milk tripeptides on blood pressure: a meta-analysis of randomized controlled trials |journal=Nutrition |volume=24 |issue=10 |pages=933–40 |doi=10.1016/j.nut.2008.04.004 |pmid=18562172}}</ref><ref>{{Cite journal |last=Pripp AH |year=2008 |title=Effect of peptides derived from food proteins on blood pressure: a meta-analysis of randomized controlled trials |journal=Food & Nutrition Research |volume=52 |article-number=10.3402/fnr.v52i0.1641 |doi=10.3402/fnr.v52i0.1641 |pmc=2596738 |pmid=19109662}}</ref> although the evidence is mixed.<ref>{{Cite journal |vauthors=Engberink MF, Schouten EG, Kok FJ, van Mierlo LA, Brouwer IA, Geleijnse JM |date=February 2008 |title=Lactotripeptides show no effect on human blood pressure: results from a double-blind randomized controlled trial |journal=Hypertension |volume=51 |issue=2 |pages=399–405 |doi=10.1161/HYPERTENSIONAHA.107.098988 |pmid=18086944 |doi-access=free}}</ref>
* Peptidic components from traditional Chinese medicine Colla Corii Asini in hematopoiesis.<ref>{{Cite journal |last1=Wu |first1=Hongzhong |last2=Ren |first2=Chunyan |last3=Yang |first3=Fang |last4=Qin |first4=Yufeng |last5=Zhang |first5=Yuanxing |last6=Liu |first6=Jianwen |date=April 2016 |title=Extraction and identification of collagen-derived peptides with hematopoietic activity from Colla Corii Asini |journal=Journal of Ethnopharmacology |volume=182 |pages=129–136 |doi=10.1016/j.jep.2016.02.019 |pmid=26911525}}</ref>
* [[Jelleine]] – produced from [[royal jelly]] of honey bees.

== Terminology ==

=== Length ===
Several terms related to peptides have no strict length definitions, and there is often overlap in their usage:{{cn|date=January 2025}}
* A ''polypeptide'' is a single linear chain of many amino acids (any length), held together by [[amide bond]]s.
* A ''[[protein]]'' consists of one or more polypeptides (more than about 50 amino acids long).
* An ''[[oligopeptide]]'' consists of only a few amino acids (between two and twenty).

=== Number of amino acids ===
[[File:Tripeptide Val-Gly-Ala Formula V1.svg|thumb|upright=1.3|A tripeptide (example [[Valine|Val]]-[[Glycine|Gly]]-[[Alanine|Ala]]) with <br /><span style="color:green;">'''green'''</span> marked [[N-terminus|amino end]] ([[Valine|<span style="color:green;">'''L-valine'''</span>]]) and <br /><span style="color:blue;">'''blue'''</span> marked [[C-terminus|carboxyl end]] ([[Alanine|<span style="color:blue;">'''L-alanine'''</span>]])]]

Peptides and proteins are often described by the number of amino acids in their chain, e.g. a protein with 158 amino acids may be described as a "158 amino-acid-long protein".
{{anchor|Notes on terminology"}}Peptides of specific shorter lengths are named using [[IUPAC numerical multiplier]] prefixes:
* A ''[[Wikt:monopeptide|monopeptide]]'' has one amino acid (not alone but combined with (an)other type(s) of molecule(s)).
* A ''[[dipeptide]]'' has two amino acids.
* A ''[[tripeptide]]'' has three amino acids.
* A ''[[tetrapeptide]]'' has four amino acids.
* A ''pentapeptide'' has five amino acids. (''e.g.'', [[enkephalin]]).
* A ''hexapeptide'' has six amino acids. (''e.g.'', [[angiotensin IV]]).
* A ''heptapeptide'' has seven amino acids. (''e.g.'', [[spinorphin]]).
* An ''octapeptide'' has eight amino acids (''e.g.'', [[Angiotensin#Angiotensin II|angiotensin II]]).
* A ''nonapeptide'' has nine amino acids (''e.g.'', [[oxytocin]]).
* A ''decapeptide'' has ten amino acids (''e.g.'', [[gonadotropin-releasing hormone]] and [[angiotensin#Angiotensin I|angiotensin I]]).
* A ''undecapeptide'' has eleven amino acids (''e.g.'', [[substance P]]).

The same words are also used to describe a group of residues in a larger polypeptide (''e.g.'', [[RGD motif]]).

=== Function ===
* 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 ''[[pepducin]]s'' 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 [[opioidergic]]s, which are [[neuropeptidergic]]s.
* A cell-penetrating peptide is a peptide able to penetrate the cell membrane.

== See also ==
{{wikiquote}}
{{Div col|colwidth=20em}}
* [[Acetyl hexapeptide-3]]
* [[Beefy meaty peptide]]
* [[Collagen hybridizing peptide]], a short peptide that can bind to denatured collagen in tissues
* [[Bis-peptide]]
* [[CLE peptide]]
* [[D-peptide]]
* [[Epidermal growth factor]]
* ''[[Journal of Peptide Science]]''
* [[Lactotripeptides]]
* [[Micropeptide]]
* [[Neuropeptide]]
* [[Palmitoyl pentapeptide-4]]
* [[Pancreatic hormone]]
* [[peptide spectral library]]
* [[Peptide synthesis]]
* [[Peptidomimetic]]s (such as [[peptoid]]s and [[beta-peptide|β-peptide]]s)  to peptides, but with different properties.
* [[Protein tag]], describing addition of peptide sequences to enable protein isolation or detection
* [[Replikins]]
* [[Ribosome]]
* [[Translation (biology)]]
{{Div col end}}

== References ==
{{Reflist}}

{{Peptides}}
{{Amino acids}}
{{Protein primary structure}}
{{Amino acid metabolism enzymes}}
{{Authority control}}

[[Category:Peptides| ]]