Editing Peptide (section)

== 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 "propeptides" 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 |last=Tao |first=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 |pages=eaam9756 |doi=10.1126/science.aam9756 |pmc=5712217 |pmid=29146781}}</ref><ref>{{Cite journal |last=Tao |first=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 |last=Tao |first=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 |last=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 |last=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 |last=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 |last=Heitz |first=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 |last=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 |pages=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 |last=Wu |first=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.