• The Korean Journal of Food And Nutrition
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• v.22 no.4
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• pp.633-638
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• 2009

In this study, pork meat oligopeptides and ISP oligopeptides were prepared from purified meat protein and, isolated soybean protein, respectively. These oligopeptides were added to porridge. Then their manufacturing suitability and quality characteristics were evaluated. The porridge which included meat oligopeptides and ISP oligopeptides satisfied the 20% RI (recommended intake) of protein and 40% RI of EAA for man between the ages of 20 to 29. According to measurements of the physicochemical characteristics of porridge, the degree of viscosity, spreadability, pH, and lightness L value, were acceptable for consumption. In addition, the oligopeptide powders had good solubility. and were easy to add when cooking. The above results indicate that pork meat oligopeptides and ISP oligopeptides are excellent dietary nitrogen sources for a variety of applications.

• The Korean Journal of Food And Nutrition
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• v.22 no.3
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• pp.416-420
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• 2009

A formula diet based on pork meat oligopeptides(pork meat protein hydrolysates) was designed for experimental hepatitic rats. The rats were given D-galactosamine for 6 days. During this period, the rats were provided with a 12% casein diet or the formula diet which was low in aromatic amino acids and rich in branched chain amino acids. The formula diet was prepared using pork meat oligopeptides as the principal nitrogen source. The hepatitic rats given the formula diet had lower plasma GOT and GPT concentrations. Additionally, the fischer ratio of the plasma was significantly lower in those rats. However, there was no significant difference in the plasma insulin-like growth factor-I concentration before and after acid-ethanol extraction among groups. These results suggest that the formula diet was better for the animals than the casein diet. Furthermore, these findings suggest that pork meat oligopeptides are an excellent material for preparation of formula diets for patients suffering from hepatitis.

• Bulletin of the Korean Chemical Society
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• v.12 no.3
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• pp.286-289
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• 1991

The changed isotropic absolute Raman intensities of the phosphate residue in the complexes of positive charge oligopeptides, lys-lys, arg-arg, lys-aromat-lys, negative charge diethyl phosphoric acid (DEP) and polyriboadenylic acid{poly(rA)} were reported and discussed. Our measurements showed that the absolute intensities of phosphate stretch vibration in complexes were different according to the reaction partners. Due to the partial electrical charge and molecular structure of oligopeptides for the complex formation lysine can interact more strongly than arginine when the reaction partners have short chain and no steric hindrance. Owing to these reasons the intensity of phosphate stretching vibration is very sensitive according to the circumstance of reaction. From our results we could suggest that we can discriminate any one of the the lysine and arginine in the complicated biological molecule during interaction between nucleotides and proteins. The activity of reaction of two basical oligopeptides is not quite similar for complex formation in aqueous solution. The activity of dipeptides depends upon the structure of molecule and environment for complex formation. Aromatic ring contributes to electrostatic interaction in complexes. The amount of the absolute intensity for pure stacking interaction is smaller than electrostatic interaction in macromolecular complexes.

• Journal of the Korean Society of Food Culture
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• v.17 no.4
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• pp.363-376
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• 2002

In order to establish the processing conditions for salt-fermented liquefaction of anchovy(Engrulis japonica), changes in the amino acid composition from oligopeptides during fermentation periods were analyzed. Experimental sample A: chopped whole anchovy, adding 20% water, heating at $50^{\circ}C$ for 9 hrs and then adding 10% NaCl. Sample B: chopped whole anchovy, adding 20% water, heating at $50^{\circ}C$ for 9 hrs and then adding 13% NaCl. Sample C: chopped whole anchovy adding 13% NaCl. Sample D: whole anchovy adding 17% NaCl. The total amino acids from oligopeptides in fermented liquefaction of anchovy increased in early fermentation period and reached highest level, and then they declined irregularly during fermentation. Their maximum amounts were just after heating at $50^{\circ}C$ for 9 hrs in sample A, after 15 days in sample B, and after 60 days in samples C and D. The fermented liquefaction of anchovy extracts were rich in glutamic acid, aspartic acid, proline, glycine, alanine, lysine and valine. However, the contents of most amino acids fluctuated by the experimental specimens and fermenting periods. Among them glutamic acid was the most abundant amino acid which was occupied $0.6{\sim}27.7%$(average 24.0%) in the content of total amino acids from oligopeptides. The contribution of the amino acid composition from oligopeptides to extractive nitrogen was occupying average 20.8 and 17.5% in rapid- and low salt-fermented liquefaction(sample A, B and C) and traditional fermented liquefaction(sample D), respectively.

• Bulletin of the Korean Chemical Society
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• v.31 no.12
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• pp.3735-3739
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• 2010

Branched oligopeptides prepared by coupling a very hydrophobic aspartic diamino acid ethyl ester such as Asp $(LeuEt)_2$, $Asp(IleEt)_2$ and $Asp(PheEt)_2$ to glycine or glycylphenylalanine were grafted to the cyclotriphosphazene backbone bearing an equimolar hydrophilic poly(ethylene glycol) (PEG). The properties of the resultant amphiphiles were examined in comparison with those of the linear oligopeptide analogues previously reported. All cyclic phosphazene trimers grafted with the branched tetra- and pentapeptides displayed a normal trend of thermosensitivity depending on their hydrophilic to hydrophobic balance, but the stability and particle size of their micelles were found to be greatly dependent on the fine structure of the branched oligopeptides grafted. The trimers bearing branched tetrapeptides with a low hydrophobicity were found to form unstable micelles initially, which reassemble into thermodynamically more stable polymersomes.

• Journal of Periodontal and Implant Science
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• v.42 no.4
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• pp.113-118
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• 2012

Purpose: The aim of this study was to investigate the effects of synthetic fibronectin (FN) fragments, including fibrin binding sites from amino-terminal FN fragments containing type I repeats 1 to 5, on osteoblast-like cell activity. Methods: Oligopeptides ranging from 9 to 20 amino acids, designated FF1, FF3, and FF5, were synthesized by a solid-phase peptide synthesizing system, and we investigated the effects of these peptides on cell attachment and extent of mineralization using confocal microscopy, 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assays, and Alizarin red S staining. Results: FF3 and FF5 peptides increased the number of attached human osteoblastic cells, and FF3 administration led to prominent cell spreading. Mineralization was increased in FF3 and FF5 compared to FF1 and the untreated control. Conclusions: Taken together, it can be concluded that the fibrin-binding oligopeptides FF3 and FF5 enhanced cell attachment and mineralization on osteoblast-like cells. These results indicate that FF3 and FF5 have the potential to increase osteoblast-like cell activity. Performing an in vivo study may provide further possibilities for surface modification of biomimetic peptides to enhance osteogenesis, thus improving the regeneration of destroyed alveolar bone.

• Journal of Periodontal and Implant Science
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• v.40 no.5
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• pp.211-219
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• 2010

Purpose: Fibronectin (FN) has been shown to stimulate bone regeneration in animal models. The aim of this study was to evaluate the capacity of bovine bone mineral coated with synthetic oligopeptides to enhance bone regeneration in rabbit calvarial defects. Methods: Oligopeptides including fibrin-binding sequences of FN repeats were synthesized on the basis of primary and tertiary human plasma FN structures. Peptide coated and uncoated bone minerals were implanted into 10 mm calvarial defects in New Zealand white rabbits, and the animals were sacrificed at 4 or 8 weeks after surgery. After specimens were prepared, histologic examination and histomorphometric analysis were performed. Results: At 4 weeks after surgery, the uncoated groups showed a limited amount of osteoid formation at the periphery of the defect and the oligopeptide coated groups showed more osteoid formation and new bone formation in the center of the defect as well as at the periphery. At 8 weeks, both sites showed increased new bone formation. However, the difference between the two sites had reduced. Conclusions: Fibrin-binding synthetic oligopeptide derived from FN on deproteinized bovine bone enhanced new bone formation in rabbit calvarial defects at the early healing stage. This result suggests that these oligopeptides can be beneficial in reconstructing oral and maxillofacial deformities or in regenerating osseous bone defects.

• Fisheries and Aquatic Sciences
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• v.2 no.2
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• pp.135-141
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• 1999

In order to investigate the composition of extractive nitrogenous components in the diploid and the triploid oysters, Crassostrea gigas, cultured at the south coast of Korea, the whole edible part (whole body) was analyzed into extractive nitrogen, free amino acids, oligopeptides, ATP and its related compounds, quaternary ammonium bases, and guanidino compounds using specimens collected from April to May of 1992. The major free amino acids in the diploid and the triploid were taurine, proline, alanine, glycine, glutamic acid hypotaurine, glutamine, arginine, aspartic acid, and $\beta-alanine$. There was no conspicuous difference in the constituents of free amino acids between the diploid and the triploid. A lot of hypotaurine was detected in the diploid and the triploid of oyster and the contents of them were 107 mg and 123 mg/100g, respectively. The compounds, glycinebetaine, homarine and trigonelline were found in both the diploid and the triploid. Among them, glycinebetaine was the most prominent in all the samples. The amount of protein, glycogen, extractive nitrogen, oligopeptides, ATP and its related compounds, and free amino acids in the triploid was higher than that of the diploid (p<0.10)

• Bulletin of the Korean Chemical Society
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• v.17 no.2
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• pp.131-138
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• 1996

The conformational transition of oligopeptide multimer,-(HPPHPPP)n-, is studied (H:hydrophobic amino acid, P:hydrophilic amino acid). The helix/coil transitions are detected in the multimer. The transition depends on the number of amino acid in the sequence, the concentration of the oligopeptide, and temperature which affects helix stability constant (${\xi}$) and hydrophobic interaction parameter (wj). In the thermodynamic equilibrium system jA${\rightarrow}$Aj (where A stands for oligopeptide monomer), Skolnick et al., explained helix/coil transition of dimer by the matrix method using Zimm-Bragg parameters ${\xi}$ and $\sigma$ (helix initiation constant). But the matrix method do not fully explain dangling H-bond effects which are important in oligopeptide systems. In this study we propose a general theory of conformational transitions of oligopeptides in which dimer, trimer, or higher multimer coexists. The partition of trimer is derived by using zipper model which account for dangling H-bond effects. The transitions of multimers which have cross-linked S-S bonds or long chains do not occur, because they keep always helical structures. The transitions due to the concentration of the oligopeptides are steeper than those due to the chain length or temperature.

• International Journal of Industrial Entomology and Biomaterials
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• v.9 no.1
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• pp.29-33
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• 2004

Low molecular weight silk fibroin (LMSF), which was prepared by hydrolysis of silk fibroin using high-temperature and high-pressure method, was found to inhibit the oxidation of L-3,4,-dihydroxyphenylalanine (L-DOPA) catalyzed by mushroom tyrosinase (EC 1.14.18.1). LMSF contained mostly free amino acids such as L-glycine, L-alanine, and L-serine and oligopeptides, mainly glycine-alanine dimer. As a result of analyzing the inhibition kinetics from Lineweaver-Burk plots, L-glycine and glycine-alanine dimer showed noncompetitive behavior while uncompetitive behavior was observed in L-alanine, and L-serine. When weight percent concentration of ${ID_50}$ was compared, L-glycine was most effective on the inhibition and LMSF was also good enough for the inhibition effect of tyrosinase activity. LMSF showed a mixed-type inhibition and the inhibitory mechanism of LMSF might be caused by free amino acids and oligopeptides. As a result of spectroscopic observation with time, initial rate of increase of DOPAchrome decreased remarkably and the time to reach maximum absorbance increased as an increase of the concentration of L-glycine, meaning that L-glycine made itself mainly responsible for the formation of chelate with ${Cu^2+}$ in tyrosinase. However, in case of L-alanine, L-serine, and especially glycine-alanine dimmer, the production of DOPAchrome after an arrival at maximum absorbance decreased, indicating the production of adducts through the reaction with DOPAquinone.