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Peptide
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"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 Gr. , "digested", derived from , "to digest") are short chains of
amino acid monomers linked by peptide (amide) bonds, the covalent chemical bonds formed
when the carboxyl group of one amino acid reacts with the amino group of another. Peptides are
distinguished from proteins on the basis of size, and as a benchmark can be understood to
contain approximately 50 amino acids or less[citation needed]. 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, oligo- and polysaccharides, etc.
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
techniques that apply to peptides versus polypeptides and proteins differ (i.e., in the specifics of
electrophoresis, chromatography, etc.), the size boundaries that distinguish peptides from
polypeptides and proteins are not hard and fast: 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"; 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).

Contents

[hide]

1 Peptide classes

2 Peptide synthesis

3 Peptides in Molecular Biology

4 Well-known peptide families in humans

o 4.1 Tachykinin peptides
o 4.2 Vasoactive intestinal peptides
o 4.3 Pancreatic polypeptide-related peptides
o 4.4 Opioid peptides
o 4.5 Calcitonin peptides
o 4.6 Other peptides

5 Notes on terminology

6 Doping in sports

7 See also

8 References

Peptide classes[edit source | editbeta]

Peptides are divided into several classes, depending on how they are produced:
Milk peptides
Milk peptides are formed from milk proteins by enzymatic breakdown by digestive
enzymes or by the proteinases formed by lactobacilli during the fermentation of milk.
Ribosomal peptides
Ribosomal peptides are synthesized by translation of mRNA. They are often subjected to
proteolysis to generate the mature form. These function, typically in higher organisms, as
hormones and signaling molecules. Some organisms produce peptides as antibiotics, such
as microcins.[1] Since they are translated, the amino acid residues involved are restricted
to those utilized by the ribosome. However, these peptides frequently have
posttranslational modifications, such as phosphorylation, hydroxylation, sulfonation,

palmitylation, glycosylation and disulfide formation. In general, they are linear, although
lariat structures have been observed.[2] More exotic manipulations do occur, such as
racemization of L-amino acids to D-amino acids in platypus venom.[3]
Nonribosomal peptides
These peptides are assembled by enzymes that are specific to each peptide, rather than by
the ribosome. The most common non-ribosomal peptide is glutathione, which is a
component of the antioxidant defenses of most aerobic organisms.[4] Other nonribosomal
peptides are most common in unicellular organisms, plants, and fungi and are synthesized
by modular enzyme complexes called nonribosomal peptide synthetases.[5] 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.[6]
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.[7]
Peptones
See also Tryptone
Peptones are derived from animal milk or meat digested by proteolytic digestion. In
addition to containing small peptides, the resulting spray-dried material includes fats,
metals, salts, vitamins and many other biological compounds. Peptone is used in nutrient
media for growing bacteria and fungi.[8]
Peptide fragments
Peptide fragments refer to fragments of proteins that are used to identify or quantify the
source protein.[9] 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.[10][11]

Peptide synthesis[edit source | editbeta]

Main article: Peptide synthesis

Solid-phase peptide synthesis on a rink amide resin using Fmoc--amine-protected amino acid

Peptides in Molecular Biology[edit source | editbeta]

Peptides have recently[citation needed] received prominence in molecular biology for several reasons.
The first is that peptides allow the creation of peptide antibodies in animals without the need to
purify the protein of interest.[12] 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 peptides have become instrumental in mass spectrometry, allowing the
identification of proteins of interest based on peptide masses and sequence. In this case the
peptides are most often generated by in-gel digestion after electrophoretic separation of the
proteins.
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.

Well-known peptide families in humans[edit source | editbeta]

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.

Tachykinin peptides[edit source | editbeta]

Substance P

Kassinin

Neurokinin A

Eledoisin

Neurokinin B

Vasoactive intestinal peptides[edit source | editbeta]

VIP (Vasoactive Intestinal Peptide; PHM27)

PACAP Pituitary Adenylate Cyclase Activating Peptide

Peptide PHI 27 (Peptide Histidine Isoleucine 27)

GHRH 1-24 (Growth Hormone Releasing Hormone 1-24)

Glucagon

Secretin

Pancreatic polypeptide-related peptides[edit source | editbeta]

NPY (NeuroPeptide Y)

PYY (Peptide YY)

APP (Avian Pancreatic Polypeptide)

PPY Pancreatic PolYpeptide

Opioid peptides[edit source | editbeta]

Proopiomelanocortin (POMC) peptides

Enkephalin pentapeptides

Prodynorphin peptides

Calcitonin peptides[edit source | editbeta]

Calcitonin

Amylin

AGG01

Other peptides[edit source | editbeta]

B-type Natriuretic Peptide (BNP) - produced in myocardium & useful in medical

diagnosis

Lactotripeptides - Lactotripeptides might reduce blood pressure,[13][14][15] although the

evidence is mixed.[16]

Notes on terminology[edit source | editbeta]

Length:

A polypeptide is a single linear chain of amino acids.

A protein is one or more polypeptides more than about 50 amino acids long.

An oligopeptide (or simply a peptide) is a polypeptide less than 30-50 amino acids long.

Number of amino acids:

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 heptapentide 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).

An undecapeptide (or monodecapeptide) has eleven amino acids, a dodecapeptide (or

didecapeptide) has twelve amino acids, a tridecapeptide has thirteen amino acids, and so
forth.

An icosapeptide has twenty amino acids, a tricontapeptide has thirty amino acids, a
tetracontapeptide has forty amino acids, and so forth.

See also: IUPAC numerical multiplier

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 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.

Doping in sports[edit source | editbeta]

The term "peptide" has been incorrectly/unclearly used to mean "illegal secretagogue" and
"peptide hormones" in sports doping matters: Illegal secretagogue peptides are classified as a
Schedule 2 (S2) prohibited substance 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 peptide secretagogues have been on the WADA prohibited substances list since at least
2008. The Australian Crime Commission (incorrectly using the term "peptides") cited the alleged
misuse of the following illegal peptide secretagogues used in Australian sport - and specifically
the Essendon Football Club:[17] CJC-1295 GhRP-6 hexarelin There is controversy on the
legality of peptide secretagogue in sports.[18] [edit]

See also[edit source | editbeta]

Antineoplaston

Argireline

Beefy meaty peptide

Bis-peptide

Epidermal Growth Factor

Journal of Peptide Science

Lactotripeptides

Pancreatic hormone

Peptide Spectral Library

Peptide synthesis

Peptidomimetics (such as peptoids and -peptides) to peptides, but with different

properties.

Protein tag, describing addition of peptide sequences to enable protein isolation or

detection

Ribosome

Translation

References[edit source | editbeta]

1.

^ Duquesne S, Destoumieux-Garzn D, Peduzzi J, Rebuffat S (August 2007). "Microcins, geneencoded antibacterial peptides from enterobacteria". Natural Product Reports 24 (4): 70834.
doi:10.1039/b516237h. PMID 17653356.

2.

^ Pons M, Feliz M, Antnia Molins M, Giralt E (May 1991). "Conformational analysis of

bacitracin A, a naturally occurring lariat". Biopolymers 31 (6): 60512. doi:10.1002/bip.360310604.
PMID 1932561.

3.

^ Torres AM, Menz I, Alewood PF, et al. (July 2002). "D-Amino acid residue in the C-type
natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus".
FEBS Letters 524 (1-3): 1726. doi:10.1016/S0014-5793(02)03050-8. PMID 12135762.

4.

^ Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry 52 (1): 71160.

doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189.

5.

^ Hahn M, Stachelhaus T (November 2004). "Selective interaction between nonribosomal peptide

synthetases is facilitated by short communication-mediating domains". Proceedings of the National
Academy of Sciences of the United States of America 101 (44): 1558590.
Bibcode:2004PNAS..10115585H. doi:10.1073/pnas.0404932101. PMC 524835. PMID 15498872.

6.

^ Finking R, Marahiel MA (2004). "Biosynthesis of nonribosomal peptides1". Annual Review of

Microbiology 58 (1): 45388. doi:10.1146/annurev.micro.58.030603.123615. PMID 15487945.

7.

^ Du L, Shen B (March 2001). "Biosynthesis of hybrid peptide-polyketide natural products".

Current Opinion in Drug Discovery & Development 4 (2): 21528. PMID 11378961.

8.

^ Payne JW (1976). "Peptides and micro-organisms". Advances in Microbial Physiology 13: 55

113. doi:10.1016/S0065-2911(08)60038-7. PMID 775944.

9.

^ Hummel J, Niemann M, Wienkoop S, et al. (2007). "ProMEX: a mass spectral reference

database for proteins and protein phosphorylation sites". BMC Bioinformatics 8: 216. doi:10.1186/14712105-8-216. PMC 1920535. PMID 17587460.

10.

^ Webster J, Oxley D (2005). "Peptide mass fingerprinting: protein identification using MALDITOF mass spectrometry". Methods in Molecular Biology 310: 22740. doi:10.1007/978-1-59259-948-6_16.
PMID 16350956.

11.

^ Marquet P, Lachtre G (October 1999). "Liquid chromatography-mass spectrometry: potential in

forensic and clinical toxicology". Journal of Chromatography B 733 (1-2): 93118. doi:10.1016/S03784347(99)00147-4. PMID 10572976.

12.

^ Bulinski JC (1986). "Peptide antibodies: new tools for cell biology". International Review of
Cytology 103: 281302. doi:10.1016/S0074-7696(08)60838-4. PMID 2427468.

13.

^ Boelsma E, Kloek J (March 2009). "Lactotripeptides and antihypertensive effects: a critical

review". The British Journal of Nutrition 101 (6): 77686. doi:10.1017/S0007114508137722.
PMID 19061526.

14.

^ Xu JY, Qin LQ, Wang PY, Li W, Chang C (October 2008). "Effect of milk tripeptides on blood
pressure: a meta-analysis of randomized controlled trials". Nutrition 24 (10): 93340.
doi:10.1016/j.nut.2008.04.004. PMID 18562172.

15.

^ Pripp AH (2008). "Effect of peptides derived from food proteins on blood pressure: a metaanalysis of randomized controlled trials". Food & Nutrition Research 52 (0). doi:10.3402/fnr.v52i0.1641.
PMC 2596738. PMID 19109662.

16.

^ Engberink MF, Schouten EG, Kok FJ, van Mierlo LA, Brouwer IA, Geleijnse JM (February
2008). "Lactotripeptides show no effect on human blood pressure: results from a double-blind randomized
controlled trial". Hypertension 51 (2): 399405. doi:10.1161/HYPERTENSIONAHA.107.098988.
PMID 18086944.

17.

^ http://www.heraldsun.com.au/sport/afl/essendon-scandal-the-story-so-far/story-fni5f6kv1226635822954

18.

^ https://theconversation.edu.au/we-need-an-advocate-against-asadas-power-in-doping-control12119

Koh, B., & Hardie, M. (2013). We need an advocate against ASADAs power in doping
control. Retrieved from https://theconversation.edu.au/we-need-an-advocate-againstasadas-power-in-doping-control-12119
[show]

Endocrine system: hormones (Peptide hormones Steroid hormones)

GnRH TRH Dopamine CRH GHRH/Somatostatin

Hypothalamus
Melanin concentrating hormone
Hypothalamic
Posterior pituitaryVasopressin Oxytocin
pituitary
(FSH FSHB, LH LHB, TSH TSHB, CGA)
Anterior pituitaryProlactin POMC (CLIP, ACTH, MSH, Endorphins,
Lipotropin) GH

Adrenal axis

Thyroid axis

Adrenal cortex: aldosterone cortisol DHEA

Adrenal medulla: epinephrine norepinephrine
Thyroid: thyroid hormone (T3 and T4) calcitonin
Parathyroid: PTH

Gonadal axis
Testis: testosterone AMH inhibin
Ovary: estradiol progesterone activin and inhibin relaxin (pregnancy)

Placenta: hCG HPL estrogen progesterone

Islet-AcinarPancreas: glucagon insulin amylin somatostatin pancreatic
Axispolypeptide
Pineal glandPineal gland: melatonin

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