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Differences between Long and Short Peptide Chains

Posted on September 30, 2013 by Maxim Peptide

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A peptide is typically defined as a chain of amino acid
monomers (that is, a molecule that may chemically attach
to other molecules to form a polymer) which are linked by
covalent bonds !hey are typically split into two "roups#
$on" chain peptides, also known as polypeptides or
proteins% and short chain peptides, sometimes referred to
as o"liopeptides
Peptides play a lar"e role within a certain subset of
biomimetic materials, which are substances developed
usin" elements that naturally occur in nature !he
particular subset of biomimetic materials that pertains to
peptides relates to tissue en"ineerin"% the process in which cells, materials, and en"ineerin" is combined with
appropriate biochemical and physio&chemical aspects to enhance, repair, or replace biolo"ical functions of tissues
found in livin" or"anisms (' (adisic, et al, )*+,&)*-.)
!he primary use of peptides in tissue en"ineerin" results from their ability to elicit responses by mimickin"
e/tracellular matri/, or 01', proteins 2n essence, by replicatin" the functionality of these proteins, peptides can
manipulate various biolo"ical functions, outside the realm of the normal physiolo"ical re"ulations, as dictated by an
or"anism3s typical processes (4hin, 5, et al, 6*+*&+*-6)
7hile both forms of peptides share some similar traits that make them essential study components, other aspects
of their behavior are uni8ue (4hin, 5, et al, 6*+*&+*-6)
!he Functionality of $on" 1hain Peptides
A lon" chain peptide is referred to as a polypeptide because it is a len"thy, continual chain of polymers made up of
many amino acids 9 typically between ): and ):: 9linked to"ether chemically $on" chain peptides have a
molecular wei"ht of up to about ):,::: "rams per mole, and can fold into specific three&dimensional confi"urations
!hese types of peptides are commonly referred to as proteins !hey are lar"ely considered to be the core
components of basic biolo"ical processes found within livin" or"anisms 4ome of the functions that proteins
perform include#
D;A replication 9 !he process of makin" two identical copies out of one ori"inal D;A molecule 2t is the
foundation for biolo"ical inheritance for all livin" or"anisms 2n essence, this is the code that determines an
or"anism3s physical makeup
1ell si"nalin" 9 !he comple/ system of communication that controls and re"ulates essential cellular activities
and coordinates a cell3s action !his sometimes falls under the parameters of respondin" to stimuli !his
communication is responsible for maintainin" an or"anism3s overall systematic functionality
0n<yme catalysis 9 !he process of controllin" the rate of a chemical reaction by speciali<ed proteins as a
means to maintain biolo"ical efficiency (= 1haturvedi, )&,)
Polypeptides re"ulate or tri""er a si"nificant amount of or"anic functions, either actin" near to or distance from the
site where they are produced and released !heir manner of re"ulation can be traced back to the hormones that
they help to e/press within the or"anism !hese hormones help to re"ulate various essential functions that enable
an or"anism to operate normally, from antidiuretic (that is, water retainin") action in the kidneys to blood su"ar
control in the pancreas (= 1haturvedi, )&,)
>ecause of their len"thy si<e, lon" chain peptides have hi"her instability than their short chain counterparts 7hile
a polypeptide contains a wealth of information within its construct, its physical structure allows for more potential
manifestations of de"radation throu"h processes such as#
5ydrolysis 9 !he process in which chemical bonds e/perience cleava"e, otherwise known as division, due to
the addition of water
(acemi<tion 9 !he process in which a conversion of an enatiomerically pure mi/ture (that is, where only one
enantiomer is present) into some sort of mi/ture where more than one enantiomers are present (=
1haturvedi, )&,)
Polypeptides can also e/perience issues pertainin" to physical de"radation dependin" upon their molecular wei"ht,
such as#
Denaturation 9!he process in which proteins or nucleic acids lose the structure that is present in their native
state due to e/ternal stress, resultin" in the disruption of cell activity or even cell death 4ome of these e/ternal
stresses include a concentrated inor"anic salt, a stron" base, a stron" acid, heat, or an or"anic solvent such as
4elf Association 9 !he process in which a lon" chain peptide interacts selectively and in a non&covalent way
within itself
=elation 9 !he process where a fluid solution is converted into a semi&solid mass composed of multiple peptide
fibrils and tan"led within a comple/ mesh
Adsoprtion 9 !he process in which atoms or ions form a "as, li8uid, or a dissolved solid to adhere to a
molecule3s surface !his process is a conse8uence of surface ener"y, which disrupts intermolecular bonds
!his process is sometimes marked with the polypeptide collapsin"
A""re"ation 9 !he process in which a protein structure creates its shape is known as protein foldin"
?ccasionally, these proteins "et mis&folded, which inhibits their proper functionality !he process of
a""re"ation relates to the erroneous process that occurs when misfolded proteins accumulate at either an
intracellular level or an e/tracellular level (= 1haturvedi, )&,)
!his hi"h level of chemical instability makes the study of polypeptides a difficult challen"e, as numerous paths of
disruption makes it difficult to obtain and determine proper and consistent clinical results
!he Functionality of 4hort 1hain Peptides
>y contrast, short chain peptides (which are sometimes known as oli"opeptides) are si"nificantly smaller chains of
amino acids !hese amino acids are se8uentially bonded to"ether to form peptide bonds !hese short peptide
chains do not contain proteins 7hile there is no definitive ma/imum number of amino acids a chain can include
and still be considered a short chain peptide, the minimum number of amino acids that must be present to be
considered a short chain peptide is only two (4citable)
4hort chain peptides, however, can share similar traits with lon" chain peptides or polypeptides For e/ample, they
both can secrete hormones, which are essential components for the overall mechanics and operations of an
or"anism (4citable) 5owever, short chain peptides do have an advanta"e over lon" chain peptides in that the
smaller chain si<e is more stable 4mall chain peptides do not e/perience some of the issues that lon" chain
peptides do because of their shorter len"th@most notably collapsin" durin" absorption Additionally, short chain
peptides can be replicated much more efficiently (4hin, 5, et al, 6*+*&+*-6) !his makes them si"nificantly more
attractive for research !he stability and efficiency of short chain peptides results in a more stable base of research
metrics from which a valid library of case studies can be created >ecause short chain peptides won3t collapse as a
result of their len"th, research done with short chain peptides provide more consistent, stable data and results
!his, in turn, provides researchers with more accurate, definitive set of data overall (4hin, 5, et al, 6*+*&+*-6)
Peptides and !issue 0n"ineerin"
!he primary focus of short chain peptide research on tissue en"ineerin" is to discover and develop biocompatible
materials to help combat natural de"radation that is part of the a"in" process
4pecificallyamino acids located within the peptides are used as buildin" blocks by other biolo"ical !hese peptides
are often referred to as Aself&assemblin" peptides,B because they can be modified to contain biolo"ically active
motifs (5olmes, )) !his enables them to replicate information derived from tissue and to reproduce the same
information independently !hus, these peptides act as buildin" blocks capable of conductin" multiple biochemical
activities@up to and includin" tissue en"ineerin"
2t should be noted that tissue en"ineerin" research currently bein" performed on both short chain and lon" chain
peptides is still in early sta"es As such, any research data or metrics relative to the peptides3 effects on tissue
en"ineerin" should only be considered as preliminary
(adisic, 'ilica% Park, 5youn"shin% =recht, 4haron% 1anni<<aro, 1hristopher% $an"er, (% VunCak&;ovkovic,
=ordana% A>iometric Approach to 1ardiac !issue 0n"ineerin",B Philosophical !ransactions# >iolo"ical 4ciences
Vol *-D, ;o )6.6, >ioen"ineerin" the 5eart (Au"ust DE, D::,% p" )*+,&)*-.)
4hin, 5% 4 Fo, and A= 'ikos% A>iomemetic 'aterials for !issue 0n"ineerin",B >iomaterials, D::*D6% p 6*+*&
1haturvedi, =unCa% AA (eport on 4tability of Polypeptides and Proteins,B >irla 2nstitute of !echnolo"y and 4cience,
Pilani ((aCasthan), Au"ust D::E, p )&,
Gyle, 4tuart% A""eli, Amalia% 2n"ham, 0ileen% 'cPherson, 'ichael F% A(ecombinant 4elf&Assemblin" Peptides as
>iomaterials for !issue 0n"ineerin"B% >iomaterials, *)(*-)% December D:):, p E*E+&E6:+
4citable, APeptide DefinitionB, wwwnaturecom/scitable/definition/peptide&*),
5olmes, !odd 1 A;ovel peptide&based biomaterial scaffolds for tissue en"ineerin"% !rends in >iotechnolo"y, Vol
D: ;o ) Fanuary D::D