• Preventive Nutrition and Food Science
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• v.5 no.3
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• pp.148-152
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• 2000

Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.630-633
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• 2003

The mussel adhesive protein Mefp-1 is a natural, strong and durable adhesive that is stable under corrosive, saline conditions. Mefp-1 is found in the marine mussel Mytilus edulis and it has a molecular weight of ca. 130,000. The primary structure is mainly composed of repeating decapetides: Ala-Lys-Pro -Ser-Tyr Hyp-Hyp-Thr-DOPA-Lys. To elucidate the mechanism by which Mefp-1 bonds to metal surfaces, we have used surface-enhanced Raman spectroscopy to study the interactions of peptides related to the Mefp-1 decapeptide repeat with gold surfaces. We have concluded that the tyrosine residue and the carboxyl terminus interact strongly with the gold surface, and that proline and hydroxyproline constrain the conformations of the peptides, thereby limiting the types of possible interactions of the functional groups with the gold surface.

• Journal of the Korean Applied Science and Technology
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• v.35 no.1
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• pp.141-150
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• 2018

Mussel byssal protein has strong adhesive capability even in wet surface. It has been reported that nine proteins in marine blue mussel, often referred to a representative mussel, contribute to form mussel byssal threads and plaques. DOPA containing two hydroxy groups called cathecol is recognized that it plays a major role in adhesion as well as cohesion process within byssal structure. In this paper, adhesion and cohesion mechanisms were introduced and evaluated by supportive literature published during last decade. Diverse applications of cathecol chemicals were also examined in terms of innovative adhesive, bioadhesive and challenging material for tissue engineering. It is noticeable that reconsideration of mussel proteins could provide the various opportunities as biomaterials.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.66-66
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• 2003

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.416-416
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• 2005

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.126-126
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• 2003

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2005.06a
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• pp.641-644
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• 2005

The study on the interaction forces of some biological materials is important to understanding biological phenomena and their application to practical purpose. This paper introduces a measuring technique for biological adhesive forces using the AFM(Atomic Force Microscope). Since no standardized thesis on adhesive forces exist, the adhesive forces is defined as adhesive forces against a hardened surface of biological materials. To grant the results are meaningful, which is based on the understanding the surface characteristics of biological materials using the AFM, a nominal value of average adhesive force per unit area should be measured. Therefore the modified AFM probe with small micro glass bead was proposed so that it can guarantee the required contact area for measuring the average adhesive forces. A pyrex glass substrate with circular patterns, which was fabricated by micromachining technique, is introduced in order to controll the contact area. The two types of mussel adhesive proteins, Celltak and recombinant-MGFP5, were tested by the proposed measuring method. The test results show that the adhesive force of the mussel adhesive proteins can be reliably measured by use of this method.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.419-419
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• 2005

• Molecules and Cells
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• v.26 no.1
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• pp.34-40
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• 2008

To express an increased level of recombinant Mefp1 (marine mussel adhesive protein) in soluble form, we constructed expression vectors encoding truncated OmpA signal peptide-Mefp1 fusion proteins. OmpA signal peptide (OmpASP) is the 21 residue peptide fragment of the 23 residue OmpA signal sequence cleavable by signal peptidase I. We successfully produced increased levels of soluble recombinant Mefp1 (rMefp1) with various deletions of OmpASP, and found that the increased expression was caused by the increased pI of the N-terminus of the fusion proteins (${\geq}10.55$). All the OmpA signal peptide segments of 3-21 amino acids in length had the same pI value (10.55). Our results suggest that the pI value of the truncated OmpASP ($OmpASP_{tr}$) play an important role in directional signaling for the fusion protein, but we found no evidence for the presence of a secretion enhancer in OmpASP. For practical applications, we increased the expression of soluble rMefp1 with $OmpASP_{tr}$ peptides as directional signals, and obtained rMefp1 with the native amino terminus (nN-rMefp1) using an $OmpASP_{tr}$ Xa leader sequence that contains the recognition site for Xa protease.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2003.05a
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• pp.27-29
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• 2003

해양생명체인 홍합(mussel)은 접착단백질(adhesive protein)을 생산, 분비함으로써 홍합 자신을 바다 속의 바위와 같은 젖은 고체표면에 단단히 부착할 수 있도록 하여 강한 파도의 충격이나 바닷속의 부력 효과에 대하여도 저항할 수 있다. 홍합접착단백질은 현재 알려진 어떠한 화학합성 접착제보다도 강력한 자연적인 접착제로 알려져 있으며 대부분의 에폭시 수지보다 두 배 정도의 커다란 인장강도를 지니고 있으면서도 휘어질 수 있는 유연성을 가지고 있는 혁신적인 물질이므로 접착제 산업계에서 매우 커다란 관심을 끌고 있다. (중략)