• 제목/요약/키워드: hexapeptide

검색결과 25건 처리시간 0.033초

Construction of a Hexapeptide Library using Phage Display for Bio-panning

  • Cho, Won-Hee;Yoo, Seung-Ku
    • Journal of Microbiology
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    • 제37권2호
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    • pp.97-101
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    • 1999
  • Random hexapeptide library on the surface of filamentous bacteriophage was constructed using the SurfZAP vector. The size of the library was approximately 105. The peptide insert was flanked by two cysteines to constrain the peptide structure with a disulfide bond. This library was screened for the topoisomerase II binding peptide. Dramatic enrichment of the fusion phage over the VCS M13 helper phage was demonstrated by bio-panning affinity selection.

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Acetyl hexapeptide 함유 크림이 안면 피부 변화에 미치는 영향 (The Effect of Cream containing Acetyl hexapeptide upon the Facial Skin)

  • 최정윤;오성천
    • 한국응용과학기술학회지
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    • 제31권1호
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    • pp.120-129
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    • 2014
  • 나이를 먹으면 피부의 구조와 생리적 기능이 계속적인 감퇴를 일으켜서 노화된다. 외적요인에 의한 노화는 장기간에 걸친 자외선의 노출로 인한 광노화와 바람, 열, 담배 등이 원인으로 내인성 노화를 촉진시키거나 그 자체도 피부노화를 유발한다. 팔미토일 올리고 펩타이드 또는 세라마이드 올리고 펩타이드는 콜라겐 생산을 자극함으로써 피부의 상층부를 재생하며 아세틸 헥사펩타이드는 피하근육과 피부를 유연하게 하여 주름을 완화하는 성분으로 보톡스 대체 항주름 성분으로 대표적인 고기능성 뷰티성분이다. 대조군과 아세틸 헥사펩타이드 함유 7%, 14%, 20% 성분을 실험 군 A, B, C로 나눠서 주름의 변화, 모공의 변화, 수분량 변화, 과각질의 변화를 분석하였다. 아세틸 헥사펩타이드 함유 성분 분석 결과 통계적으로 주름과 모공, 수분에는 대조군에 비해 영향을 준 것으로 보이며, 과각질의 제거에서는 대조군과 실험군의 값에서 비슷한 결과를 얻을 수 있어 피시험자의 자가 평가의 만족도에서 주름과 모공, 수분에는 대조군에 비해 영향을 준 것으로 보이며, 과각질의 제거에서는 대조군과 실험군의 값에서 비슷한 결과를 얻었다.

Purification and Characterization of Farnesyl Protein Transferase from Bovine Testis

  • Ryo, Kwon-Yul;Baik, Young-Jin;Yang, Chul-Hak
    • BMB Reports
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    • 제28권3호
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    • pp.197-203
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    • 1995
  • Famesyl protein transferase involved in the first step of post-translational modification of $p21^{ras}$ proteins transfers the famesyl moiety from famesyl pyrophosphate to a cysteine residue in $p21^{ras}$ proteins. The enzyme was first purified 30,000-fold from bovine testis by use of 30~50% ammonium sulfate fractionation, DEAE-Sephacel ion exchange chromatography, Sephacryl S-300 gel filtration chromatography, Sephacryl S-200 gel filtration chromatography, and hexapeptide (Lys-Lys-Cys-Val-Ile-Met) affinity chromatography. The molecular weight of the purified enzyme was estimated to be ~100 kDa by gel filtration and SDS-polyacrylamide gels showed two closely spaced bands of ~50 kDa protein. These indicate that the enzyme consists of two nonidentical subunits, a and 13, which have slightly different molecular weights. The enzyme was inhibited by hexapeptide (Lys-Lys-Cys-Val-Ile-Met), which acted as an alternative substrate that competed for famesylation. Kinetic analysis by measuring initial velocities showed that famesyl protein transferase is a very slow enzyme. EDTA-treated famesyl protein transferase showed little activity with $Mg^{2+}$ or $Zn^{2+}$ alone, but required both $Mg^{2+}$ and $Zn^{2+}$ for the catalytic activity.

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B16F10 멜라닌 세포에서 신규 헥사펩타이드의 MITF 조절을 통한 멜라닌 생성 저해 효과 (Inhibitory Effects of Novel Hexapeptide on Melanogenesis by Regulating MITF in B16F10 Melanoma Cells)

  • 이응지;김잔디;정민경;이영민;정용지;김은미
    • 대한화장품학회지
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    • 제46권1호
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    • pp.11-22
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    • 2020
  • 본 연구에서는 6 개의 아미노산으로 이루어진 헥사펩타이드(hexapeptide)의 미백 효능에 대해 수행하였다. 실험 결과 헥사펩타이드 처리에 의해 유의한 수준의 멜라닌 생성 저해가 관찰 되었고, 멜라닌 생성 과정에 관여하는 주요 효소인 tyrosinase의 활성이 농도 의존적으로 억제됨이 관찰 되었다. 멜라닌 생성 관련 인자들의 발현을 관찰 한 결과 tyrosinase (TYR), tyrosinase-related protein 1 (TYRP1) 및 이들의 상위 전사인자인 microphthalmia-associated transcription factor (MITF)의 발현이 헥사펩타이드 처리에 의해 유의한 수준으로 저해 되었다. 또한 헥사펩타이드 처리에 의해 MITF 발현을 조절하는 상위 전사인자인 cAMP-response element binding protein (CREB)의 인산화가 저해 되었고 MITF 인산화를 통해 프로테아좀 분해(proteasomal degradation)를 유도하는 extracellular signal-regulated kinase (ERK) 인산화가 증가 되었다. 이외에도, 멜라노좀의 세포 내 이동에 관여하는 복합체의 구성 인자들로 알려진 Rab27A, melanophilin, myosinVa의 발현도 헥사펩타이드에 의해 유의한 수준으로 저해 되었다. 이 결과를 통해, 본 연구의 헥사펩타이드는 멜라닌세포의 멜라닌 생성 관련 핵심 전사인자인 MITF의 발현 및 분해 조절을 통해 멜라닌 생성 억제 및 멜라노좀 이동과 같은 전반적인 멜라노좀 성숙 과정에 저해 효과를 나타내는 것으로 보인다. 헥사펩타이드의 이러한 미백 효능은 신규 미백 기능성 화장품 소재로 응용될 수 있을 것으로 기대된다.

Selection of Small Synthetic Antimicrobial Peptides Inhibiting Xanthomonas citri subsp. citri Causing Citrus Canker

  • Choi, Jeahyuk;Park, Euiho;Lee, Se-Weon;Hyun, Jae-Wook;Baek, Kwang-Hyun
    • The Plant Pathology Journal
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    • 제33권1호
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    • pp.87-94
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    • 2017
  • Citrus canker disease decreases the fruit quality and yield significantly, furthermore, emerging of streptomycin-resistant pathogens threatens the citrus industry seriously because of a lack of proper control agents. Small synthetic antimicrobial peptides (AMPs) could be a promising alternative. Fourteen hexapeptides were selected by using positional scanning of synthetic peptide combinatorial libraries. Each hexapeptide showed different antimicrobial spectrum against Bacillus, Pseudomonas, Xanthomonas, and Candida species. Intriguingly, BHC10 showed bactericidal activity exclusively on Xanthomonas citri subsp. citri (Xcc), while BHC7 was none-active exclusively against two Pseudomonas spp. at concentration of $100{\mu}g/ml$ suggesting potential selectivity constrained in hexapeptide frame. Three hexapeptides, BHC02, 06 and 11, showed bactericidal activities against various Xcc strains at concentration of $10{\mu}g/ml$. When they were co-infiltrated with pathogens into citrus leaves the disease progress was suppressed significantly. Further study would be needed to confirm the actual disease control capacity of the selected hexapeptides.

Octapeptide (Alanine Angiotensin) 의 合成 (Synthesis of an Octapeptide (Alanine Angiotensin))

  • 박원길
    • 대한화학회지
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    • 제5권1호
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    • pp.33-37
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    • 1961
  • We have shown that carboxy-peptidase destroys the biological activity of angiotensin octa-and deca-peptides. Since Proline occurs as the seventh amino acid from the amino end of the chain and since carboxypeptidase does not cleave proline from a peptid chain, it is evident that the heptapeptid H.asp-arg-val-tyr-ileu-his-pro.OH is formed by this hydrolysis. This peptide must then be biologically inactive. In order to determine whether the phenyl group of the C-terminal amino acid was the necessary requirement for biological activity of the octapeptide, $ala^8$ angiotensin octapeptide(amino acids of peptides numbered from amino end) was synthesized. For this synthesis the four dipeptides were prepared: carbobenzoxy-L-prolyl-L-alanine-P-nitrobenzyl-ester, m.p. $134-135^{\circ}C,$ carbobenzoxy-L-isoleucyl-imidazole benzyl-L-histidine methyl ester, m.p. $114-116^{\circ}C,$ carbobenzoxy-L-valyl-L-tyrosine hydrazide and carbobenzoxy B-benzyl-L-aspartyl-nitro-L-arginine. The first three dipeptides were obtained as crystalline compounds. Imidazole-benzyl-L-histidine was used in the hope that it would block the histidine imidazole against side reactions in steps subsequent to the formation of the C-terminal tetrapeptide. Also, it was through that the imidazole benzylated peptides would be easier to crystallize. This, however, was not the case. The tetrapeptide, carbobenzoxy-L-isoleucyl-L-im, benzyl-histidyl, L-prolyl-L-alanine-nitrobenzyl ester was not obtained in a crystalline form. Neither could the mono-or dihydrobromide of the tetrapeptide free base be induced to crystallize. Carbobenzoxy-L-valyl-L-tyrosine azide was condensed with the tetrapeptide free base to yield the protected hexapeptide; carbobenzoxy-L-valyl-L-tyrosyl-L-isoleucyl-L-im, benzyl, histidyl-L-Prolyl-L-alanine-nitrobenzyl ester. Upon removal of the carbobenzoxy group with hydrogen bromide in acetic acid an amorphous free base hexapeptide ester was obtained. This compound gave the correct C, H, N analysis and contained the six amino acids in the correct ratio. The octapeptide was obtained by condensing this hexapeptide with carbobenzoxy-B-benzyl-L-aspartyl-nitro, L-arginine using the mixed anhydride method of condensation. This amorphous product was proven to be homogenous by chromatography in two solvent systems and upon hydrolysis yielded the eight amino acids in correct ratio. The five protecting groups were removed from the octapeptide by hydrogenolysis over palladium black catalyst. Biological assay of the free peptide indicated that it possessed less than 0.1 per cent of both pressor and oxytocic activity of the phenylalanine8 angiotensin. This suggests that the phenyl group is a point of attachment between angiotensin and its biological receptor site.

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Farnesyl protein transferase 방해제 연구를 통한 항암제의 개발

  • 이상규;박세연;백영진;최희정;양철학
    • 한국응용약물학회:학술대회논문집
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    • 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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    • pp.180-180
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    • 1994
  • Farnesyl protein transferase는 Ras precursor의 C-terminal에 있는 cystein residue에 farnesyl group을 결합시키는 효소다. 이 효소를 bovine testis에서 30-50% ammonium sulfate fractionation, DEAE-sephacel ion exchange, Sephacryl s-300 gel filtration, hexapeptide(KKCVIM) affinity chromatography를 통해 30000배로 분리하였다. 분리된 효소는 gel filtration시 약 100kDa으로, SDS-polyacrylamide 전기영동시 50kDa의 인접한 두 bands로 나타났고 이것은 $\alpha$, $\beta$ subunits으로 생각되었다. $\alpha$ subunit을 encoding하는 RAM2 유전자를 site directed mutagenesis로 145번의 histidine을 aspartate로, 140번의 aspartate를 asparagine 으로 바꾸었더니 optimal pH와 $K_{m}$ 값이 변했다. Diethyl pyrocarbonate로 histidine residues를 chemical modification시켰을때 효소의 활성이 저하되었다. 145번 histidine이 aspartate로 바뀐 돌연변이효소에서 비교적 느리게 활성이 저하되므로 145번 histidine이 이 효소의 active site에 있을것으로 추측된다.

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Identification of to Hexapeptides that Render C2 Myoblasts the Resistant Menadione-induced Cell Death

  • Hwang, Sung-Ho;Kim, Min-Jeong;Lim, Jeong-A;Woo, Joo-Hong;Kim, Hye-Sun
    • Animal cells and systems
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    • 제12권1호
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    • pp.35-39
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    • 2008
  • Menadione induced cell death in cultured C2 myoblasts. By screening synthetic peptide libraries composed of random sequence of hexapeptides, we identified the hexa-peptides pool of(Ala/Ile)-(Ile/Met)-Val-Ile-Asp-(Met/Ser)-$NH_2$ that protected the myoblasts against menadioneinduced cell death. Pre-incubation with the hexapeptide pool reduced the number of cells detached from culture dish substrate and increased the ratio of relative viability against menadione. In addition, the peptides strongly increased the expression of Bcl-2, an anti-apoptotic protein. These results suggest that the hexapeptides might enhance the resistance to cell death against menadione by increasing the expression of Bcl-2.

Structural basis of Shank PDZ interaction with the C-terminal peptide of GKAP protein and the mode of PDZ domain dimerization

  • Im, Young-Jun;Lee, Jun-Hyuck;Park, Seong-Ho;Park, Seong-Hwan;Park, Soo-Jeong;Kang, Gil-Bu;Kim, Eunjoon;Eom, Soo-Hyun
    • 한국결정학회:학술대회논문집
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    • 한국결정학회 2003년도 춘계학술연구발표회
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    • pp.14-14
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    • 2003
  • We have crystallized and determined the structures o the Shank PDZ domain, alone and in complex with the synthetic C-terminal hexapeptide of GKAP protein at resolutions of 1.8Å and 2.5Å, respectively. The structure revealed the structural basis of the ligand recongition by Class I PDZ-ligand interaction. Moreover, dimeric structureof shank PDZ domain suggests that the βA strand is a common surface for dimerization of PDZ domains.

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