BLBS102-c36 BLBS102-Simpson March 21, 2012 18:47 Trim: 276mm X 219mm Printer Name: Yet to Come
36 Biological Activities and Production of Marine-Derived Peptides 691American lobster (Homarus americanus) exhibited bacterio-
static activity against some gram-negative bacteria and both
protozoastatic and protozoacidal activity against two scutic-
ociliate parasitesMesanophrys chesapeakensisandAnophry-
oides haemophila(Battison et al. 2008). Furthermore, antimi-
crobial activity and growth inhibition of bacteria such asE. coli,
Pseudomonas aeruginosa,Bacillus subtilis, and fungi such as
Botrytis cinerea,andPenicillium expansumhave been reported
by antimicrobial peptide, CgPep33, derived from oyster (Cras-
sostrea gigas) (Liu et al. 2008). In addition, Lee and Susumu
(1998) isolated two peptides, Leu–Leu–Glu–Tyr–Ser–Ile and
Leu–Leu–Glu–Tyr–Ser–Leu, from thermolysin hydrolysate of
oyster,C. gigasthat inhibited HIV-1 protease. Moreover, an
active peptide, Arg–Arg–Trp–Trp–Cys–Arg–X (where X is an
amino acid or an amino acid analog) isolated from the enzymatic
hydrolysate of oyster,C. gigas,showed high inhibitory activity
on herpes virus (Zeng et al. 2008). In general, these AMPs are
characterized by relatively short cationic peptides with common
features, including (1)α-helices, (2)ß-sheet and small proteins,
(3) peptides with thio-ether rings, (4) peptides with an over-
representation of one or two amino acids, (5) lipopeptides, and
(6) macrocyclic cystine knot peptides (Epand and Vogel 1999).
Their modes of action are based on interaction with the mi-
crobial cellular lipid bilayer and eventual disintegration of the
cell membrane (Hwang et al. 2010). In addition to antimicrobial
action, AMPs have demonstrated diverse biological effects, all
of which participate in the control of infectious and inflamma-
tory diseases (Kamysz et al. 2003, Guan ́ı-Guerraa et al. 2010).
Therefore, there are several potential applications of AMPs to
develop new strategies or substitute the existing ones for more
sustainable and promising future of these peptides.Calcium Binding PeptidesCalcium is an important mineral for the human body. Generally,
the principal sources of calcium are milk and other diary
products (Anderson and Garner 1996). Casein phosphopeptides
(CPP) obtained after intestinal digestion of casein enhance bone
calcification (Tsuchita et al. 1993). CPP have the capacity of
chelating Ca and preventing the precipitation of Ca phosphate
salts, resulting in the increased availability of soluble Ca for
absorption (Berrocal et al. 1989, Yuan and Kitts 1994). How-
ever, some groups of people do not drink milk due to lactose
indigestion and intolerance. Therefore, peptides from other
sources, especially from aquatic source can be an alternative
for use in food to increase Ca solubility and bioavailability.
Bone oligopeptides with high affinity to calcium was prepared
from hoki bone with the aid of tuna intestine crude enzyme,
which was able to degrade hoki bone matrices comprising
collagen, noncollagenous proteins, carbohydrates, and minerals
(Jung et al. 2005). Fish bone phosphopeptides (FBP) containing
23.6% phosphorus and a molecular weight (MW) of 3.5
kDa could solubilize calcium (Jung et al. 2005). Fish bone
peptide II (FBP II) with a high content of phosphopeptide
from hoki bone could inhibit the formation of insoluble Ca
salts. The levels of femoral total Ca, bone mineral density, and
strength were increased in ovariectomized rats fed with FBPII diet (Jung et al. 2006b). Alaska pollack backbone peptide,
Val–Leu–Ser–Gly–Gly–Thr–Thr–Met–Ala–Met–Ala–Met–Tyr
–Thr–Leu–Val with the MW of 1442 Da, prepared using
pepsin hydrolysis showed affinity for calcium ions on the
surface of hydroxyapatite crystals. The peptide could solubilize
calcium at levels similar to that by casein phosphopeptide (Jung
et al. 2006a). Furthermore, calcium binding peptide derived
from pepsinolytic hydrolysate of hoki frame was identified as
Val–Leu–Ser–Gly–Gly–Thr–Thr–Met–Tyr–Ala–Ser–Leu–Tyr–
Ala–Glu with MW of 1561 Da (Jung and Kim 2007). There-
fore, fish bone oligophosphopeptide could be used as the
nutraceutical to increase the absorption of calcium.Anticoagulant ActivityAn anticoagulant therapy is a type of medication that may be
used to prevent blood from coagulating or clotting. Blood clot-
ting could be life-threatening for patients with atherosclerosis
and related cardiovascular diseases, the leading cause of heart
attack, stroke, and death (Libby 2002, Levi et al. 2003, Schultz
et al. 2003). The mainstays of clinical anticoagulant treatments
are heparin, which is a cofactor of plasma-derived and naturally
occurring inhibitors of thrombin, and coumarins that antagonize
the biosynthesis of vitamin K-dependent coagulation factors.
Although effective and widely used, heparins and coumarins
have practical limitations because their pharmacokinetics
and anticoagulation effects are unpredictable, with the risk
of many undesirable side effects, such as hemorrhaging and
thrombocytopenia resulting in the need for close monitoring of
their use. More seriously, heparins are involved in many aspects
of cellular physiology (Kakkar 2003), making their long-term
uses as anticoagulants plagued with potential side effects. The
anticoagulant marine-derived bioactive peptides have rarely
been reported, but have been isolated from marine organisms
such as marine echiuroid worm (Jo et al. 2008), starfish
Koyama et al. 1998), and blue mussel (Jung and Kim 2009).
Moreover, marine anticoagulant proteins have been purified
from blood of ark shell (Jung et al. 2001) and yellowfin sole
Rajapakse et al. 2005a). The anticoagulant activity of the above
peptides has been determined by prolongation of activated
partial thromboplastin time (APTT), prothrombin time PT) and
thrombin time assays and the activity was compared with hep-
arin, the commercial anticoagulant. The anticoagulant peptide
Gly–Glu–Leu–Thr–Pro–Glu–Ser–Gly–Pro–Asp–Leu–Phe–Val–
His–Phe–Leu–Asp–Gly–Asn–Pro–Ser–Tyr–Ser–Leu–Tyr–Ala–
Asp–Ala–Val–Pro–Arg, isolated from marine echiuroid worm,
effectively prolonged the normal clotting time on APTT
from 32.3 ± 0.9 to 192.2 ± 2.1 seconds in a dose-
dependent manner (Jo et al. 2008). This peptide binds
specifically with clotting factor FIXa, a major component
of the intrinsic tenase complex. An anticoagulant peptide
Glu–Ala–Asp–Ile–Asp–Gly–Asp–Gly–Gln–Val–Asn–Tyr–Glu
–Glu–Phe–Val–Ala–Met–Met–Thr–Ser–Lys, derived from blue
mussel, showed prolongation of 321±2.1 seconds clotting
time on APTT (from 35.3±0.5 seconds of control) and 81.3±
0.8 seconds clotting time on TT (from 11.6±0.4 seconds
of control), respectively (Jung and Kim 2009). In addition, a