• 한국식품영양학회지
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• 제22권4호
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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.

• 한국어업기술학회:학술대회논문집
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• 한국어업기술학회 2002년도 춘계 수산관련학회 공둥학술발표회
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• pp.164-165
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• 2002

• 통합자연과학논문집
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• 제9권2호
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• pp.86-93
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• 2016

The peptide sequences, GHK(Gly-His-Lys) and KTTKS(Lys-Thr-Thr-Lys-Ser), using a collagen stimulator recently were manipulated at N-terminal as a multifunctional peptide derivative with PEG(polyethyleneglycol) linker connected to gallic acid which presents anti-inflammatory activity. The multifunctional peptide derivatives were obtained in a normal peptide preparation method through SPPS(solid phase peptide synthesis) using Fmoc chemistry and a carboxyl group insertion reaction of PEG-3,4,5-triacetoxy benzoate by using potassium tert-butoxide and ethyl bromoacetate, which was separated by Sephadex DEAE. It gave a good compromise to a cosmetic application for cell cytotoxicity, anti-wrinkle, and anti-inflammation.

• 동아시아식생활학회지
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• 제19권1호
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• pp.45-51
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• 2009

In this study, food protein hydrolysates were prepared from six types of food protein: purified meat protein, whole egg protein, casein, isolated soy protein, concentrated rice protein, and gluten. Food proteins were hydrolyzed with pepsin and ethanol (80%)-soluble fractions of pepsin hydrolysates were employed for analysis. The products were colorless and odorless powders with low fat content and good solubility. The MW (molecular weight) of the protein hydrolysates was confirmed to be $200{\sim}1,800$ via gel filtration. Free amino acid contents accounted for less than 5% of the samples. The results of our amino acid analysis revealed that all food protein hydrolysates preserved their original amino acid compositions and nutritional values of their source proteins with highly pure oligopeptide mixtures. These results show that the food protein hydrolysates prepared in these investigations should prove excellent dietary nitrogen sources for a variety of applications.

• Bulletin of the Korean Chemical Society
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• 제31권12호
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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.

• Bulletin of the Korean Chemical Society
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• 제26권4호
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• pp.679-681
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• 2005

• Applied Biological Chemistry
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• 제30권1호
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• pp.88-94
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• 1987

인삼 성분중 생리적 활성을 가지고 있는 oligopeptide를 검출하고 분리하기 위하여 물 추출액을 ultra-filtration 한 후 gel filtration, ion-exchange chromatography 및 thin layer chromatography 등을 행하였다. 인삼 물 추출액으로부터 고분자 물질을 제거한 ultra-filtrate는 epinephrine에 의해 유도된 fat cell의 lipolysis를 저해하는 antilipolytic activity를 보유하고 있었으며 Sephadex G-25 gel filtration에 의해 3개 fraction으로 나뉘어졌다. 이중 첫번째 fraction(S-FI)만이 peptide 성분을 함유하고 있었으며 saponin 및 당도 검출되었다. S-FI fraction은 $Dowex\;50{\times}2\;ion-exchange\;chromatography$에 의하여 6개의 $fraction(P-F1{\sim}P-F6)$으로 분리되었고 TLC검정 결과 P-F2 fraction이 peptide fraction으로 antilipolytic를 보유하고 있었으며 TLC로 분리한 6개 spot는 각각 가수 분해한 전후의 TLC pattern을 비교해 본 결과 모두 oligopeptide임이 밝혀졌다. S-FI fraction에 존재한 saponine과 당은 P-F1 fraction 에서 모두 용출되었다.

• 대한화학회지
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• 제39권10호
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• pp.776-782
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• 1995

.alpha. 트로포마이신솨 파라마이신등은 .alpha. 나선-사슬이합체를 이룰수 있다. 사슬이합체의 나선에서 코일로의 전이 현상을 적절이 설명할수 있는 이론을 얻을 수 있었다. 이전의 이론은 Zimm-Bragg 매개변수를 사용하는 행렬식으로 올리고펩티드 사슬 이합체의 전이를 설명하였지만 이 이론으로는 올리고펩티드에서 무시할 수 없는 dangling H-bond를 고려할 수 없었다. 본 이론에서는 dangling H-bond까지 고려할수 있는 zipper 모형을 사용하였다. 나선도를 단일 사슬에서 사용되는 나선 개시상수(.sigma.), 나선 안정화(.zeta.)와 소수성상호 인력 매개변수(.omega.) 등의 함수로서 계산할 수 있었다. .alpha. 트로포마이신에서 나선 안정화의 경향을 계산 하였다. 이 올리고펩티드의 온도, 올리고펩티드의 온도, 올리고펩티드농도 변화에 의한 전이는 사슬의 해리와 동시에 일어난다. S-S 결합 등으로 이어진 사슬이 합체나 긴 사슬을 가지는 폴리펩티드는 항상 나선구조로 존재하여 전이가 일어나기 힘들다. 올리고펩티드의 농도에 의한 전이는 사슬의 길이 또는 온도계에 의한 전이보다 급격함을 알 수 있었다.

• Journal of Periodontal and Implant Science
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• 제40권5호
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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.

• 대한화학회지
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• 제40권6호
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• pp.394-400
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• 1996

결합성 사슬이합체를 형성할 수 있는 올리고펩티드-$(HPPHPPP)_n$-(H: 소수성 아미노산, P: 친수성 아미노산)는 온도, 수소이온 농도, 이온세기, 변성시약 등에 의해 구조적인 변화가 가능하다. 본 연구에서는 변성시약과 온도에 의한 올리고펩티드의 전이 현상을 이론적으로 고찰하였다. 사슬이합체로는 올리고펩티드20R, 변성시약으로는 구아니듐-염산을 사용하였다(20R에는 사슬 내의 정전기적 반발력이 10개가 존재하고, 사슬사이의 정전기적 반발력이 10개가 존재한다). 변성 시약에 의한 올리고펩티드의 나선에서 코일로의 전이는 급격한 것으로 보아, 변성이 일어나는 전이상태에서 올리고펩티드들은 완전한 나선구조와 무질서한 코일구조로만 되어있다. 반면에 온도에 의한 전이는 변성시약에 의한 전이보다 완만하게 일어난다. 낮은 온도에서 긴 나선 구조를 가지는 올리고펩티드가 짧은 나선 구조를 가지는 것보다 다량으로 존재한다. 온도가 증가할수록 부분적으로 변성된 분자들의 몰분율이 증가하여, 전이가 일어나는 온도에서 부분적으로 변성된 올리고펩티드가 널리 분포되어 있다.