• 제목/요약/키워드: disulfide bonds

검색결과 66건 처리시간 0.022초

Design and decoration of heparin on porous nanosilica via reversible disulfide linkages for controlled drug release

  • Nguyen, Dai Hai
    • 전기전자학회논문지
    • /
    • 제21권3호
    • /
    • pp.320-330
    • /
    • 2017
  • Porous nanosilica (PNS) has been identified as a potential candidate for controlled drug delivery. However, unmodified PNS-based carriers exhibited an initial release of loaded bioactive agents, which may limit their potential clinical applications. In this study, the surface of PNS was functionalized with adamantylamine (ADA) via disulfide bonds (-S-S-), PNS-S-S-ADA, which was then modified with cyclodextrin (CD)-heparin (Hep) (CD-Hep), PNS-S-S-CDH, for redox triggered rhodamine B (RhB) delivery. The obtained samples were then characterized by proton nuclear magnetic resonance ($^{1}H\;NMR$), Fourier transform infrared (FTIR), and transmission electron microscope (TEM). These results showed that PNS-S-S-CDH was successfully formed with spherical shape and average diameter of $45.64{\pm}2.33nm$. In addition, RhB was relatively encapsulated in the PNS-S-S-CDH (RhB@PNS-S-S-CDH) and slowly released up to 3 days. The release of RhB, in particular, was triggered due to the cleavage of -S-S- in the presence of dithiothreitol (DTT). It might be anticipated that the modified PNS can be used as redox-responsive drug delivery system in cancer therapy.

단백질 가수분해 효소 및 이황화 결합 환원제 처리가 밥의 텍스처에 미치는 영향 (Effect of Protease and Disulfide Bond Reducing Agent Treatment on the Texture of Cooked Rice)

  • 김성란;안승요
    • Applied Biological Chemistry
    • /
    • 제38권6호
    • /
    • pp.563-569
    • /
    • 1995
  • 쌀 단백질이 밥의 식미와 텍스쳐에 미치는 영향을 밝히기 위하여 단백질 가수분해 효소와 이황화결합 환원제 처리가 밥의 텍스쳐에 미치는 효과에 대하여 시험하였다. 세 품종의 찰밥의 경도, 부착성, 탄력성 등은 유의한 차이가 있었다. 그 중 IR 36의 밥이 가장 단단하고 부착성이 적었다. 밥의 경도는 $4^{\circ}C$에서 12시간 저장한 후에 두드러지게 증가하였으며 경도와 부착성에 대한 품종별 차이가 뚜렷하였다. 단백질 가수분해 효소를 처리한 밥과 2-mercaptoethanol을 처리한 밥은 처리하지 않은 밥보다 밥의 수분 함량과 평윤 크기가 증가하였으며 경도의 감소와 부착성의 증가가 뚜렷하였고 관능검사에 의한 기호도가 향상되었다.

  • PDF

첨가물질에 따른 알파-락트알부민 겔의 총 유리 SH 그룹, Half-Cystine 및 S-S 결합 함량 (Total Free SH Groups, Half Cystine and S-S Bond Contents of $\alpha$-Lactalbumin Gels by Various Additives)

  • 박인덕;홍윤호
    • 한국식품영양과학회지
    • /
    • 제25권6호
    • /
    • pp.922-927
    • /
    • 1996
  • 본 연구에서는 열처리에 의한 $알파-락트알부민(\alpha-La)겔의$ 특성을 규명하기 위하여 겔형성에 관여하는 인자들 즉, 염의 종류와 농도, pH, $\alpha-La$ 농도, 티올시약(NEM, Dn)의 농도를 각각 변화시켜 $90^{\circ}C에서$ 40분간 가열하여 만든 알파-락트알부민 겔의 총유리 SH그룹, half-cystine 함량, S-S 결합 함량을 측정하였다. 총 유리 SH 그룹, half-cystine 함량, S-S 결합은 첨가된 염의 종류와 농도 변화에는 큰 의존성을 나타내지 않았다. pH 2.5~3.5에서는 SH 그룹의 반응성이 낮아 pH 6.5~8.5에서의 총 유리 SH 그룹 보다 함량이 더 높고 half-cystine 함량은 일정하였으나 형성된 S-S 결합은 더 낮아 pH가 증가할수록 SH산화속도와 겔망상 구조의 형성 이 가속화됨을 확인할 수 있었다. $\alpha-La의$ 농도 증가로 half-cystine 함량은 큰 변화가 없었으나 총 유리 SH 그룹은 약간 감소하고 S-S 결합은 약간 증가하여 $\alpha-La의$ 농도 증가에 따라 겔지지체에서 S-S 결합의 관여가 큼을 나타내었다. NEM첨가의 경우는 총 유리 SH그룹과 half-cystine 함량이 급격히 감소하였으나 S-S 결합은 증가하여 NEM 첨가로 SH그룹이 반응성을 잃어 결국 $\alpha-La의$ 겔형성에 지장을 줌을 확인하였다. DTT 첨가로는 새로운 분자간 티올-이황화물 상호교환반응이 용이하게 되어 총 유리 SH 그룹은 낮고 S-S 결합은 높은 함량을 나타내었다.

  • PDF

명태 냉동 고기풀의 gel 성상 변화 (Changes of Properties of Gel from Frozen Alaska Pollack Meat Paste)

  • 정우진;박성민;이강호;이근태
    • 한국수산과학회지
    • /
    • 제26권2호
    • /
    • pp.133-140
    • /
    • 1993
  • 어육연제품의 제조시 가열에 의한 gel화 및 물성을 연구하기 위하여 소수성잔기의 노출 및 SH기의 증감 등 단백질의 성상변화를 측정하였다. 표면소수성 잔기는 $5{\sim}65^{\circ}C$의 범위에서는 온도의 상승에 따라 증가하였으며, $25{\sim}35^{\circ}C$의 온도범위에서 가장 급속히 증가하여 $35^{\circ}C$에는 처음의 약 2배로 증가하였다. 총SH기는 온도의 상승에 따라 감소하여 $85^{\circ}C$에는 처음의 약 $80\%$로 되었으며, $45^{\circ}C$부터 감소속도가 크게 나타난 바니면, 유리 SH기는 $45^{\circ}C$ 이상의 가열에 의해 크게 증가하였다. 이상의 결과들로 미루어 보아 소수성결합은 setting온도에 해당되는 $35^{\circ}C$ 전후에서 주로 형성되며, disulfide결합은 그보다 높은 $45^{\circ}C$ 이상에서 주로 형성됨을 알 수 있었다. 따라서 2단가열을 행함으로써 탄력이 증가되는 원인은 setting과정에서의 소수성결합에 의한 균일한 망상구조의 형성과 본 가열에 의한 disulfide결합의 형성에 기인하는 것으로 추정된다.

  • PDF

Stability and Cytotoxicity of Fab-Ricin A Immunotoxins Prepared with Water Soluble Long Chain Heterobifunctional Crosslinking Agents

  • Woo, Byung-Ho;Lee, Jung-Tae;Park, Myung-Ok;Lee, Kang-Ro;Han, Jeung-Whan;Park, Eun-Seok;Yoo, Sun-Dong;Lee, Kang-Choon
    • Archives of Pharmacal Research
    • /
    • 제22권5호
    • /
    • pp.459-463
    • /
    • 1999
  • The effects of the hindered and non-hindered water soluble long-chain disulfide bonds on the stability and cytotoxicity of the ricin A chain (RTA) immunotoxin were examined. The RTA immunotoxins were prepared with the Fab fragments of anti-common acute lymphoblastic leukemia antigen (CALLA) monoclonal antibody (Fab-RTA) using sulfosuccinimidyl-6-[(-methyl-(-2-pyridyldithio)toluamido]toluamido]hexanoate (S-LC-SMPT) and sulfosuccinimidyl-6-[3-(2-pyridyldithio-propionamido]hexanoate (S-LC-SPDP). The prepared Fab-RTA immunotoxins were evaluated for their conjugation yield, immunoreactivity, thermal and disulfide bond stability and cytotoxicity. The conjugation yield of the Fab-RTA immunotoxin from the water soluble long chain crosslinking agents, S-LC-SMPT and S-LC-SPDP, were comparable. Both Fab-RTA immunotoxins exhibited a similar immunoreactivity and thermal stability in aqueous solution. However, S-LC-SMPT -mediated Fab-RTA, sterically hindered, showed an enhanced disulfide bond stability in vitro over S-LC-SPDP mediated one. In the cytotoxicity against antigenic cell Daudi, the S-LC-SMPT -mediated RTA immunotoxin maintained a comparable cytotoxicity, compared with S-LC-SPDP mediated Fab-RTA immunotoxin.

  • PDF

Nucleotide Triphosphates Inhibit the Degradation of Unfolded Proteins by HslV Peptidase

  • Lee, Jung Wook;Park, Eunyong;Bang, Oksun;Eom, Soo-Hyun;Cheong, Gang-Won;Chung, Chin Ha;Seol, Jae Hong
    • Molecules and Cells
    • /
    • 제23권2호
    • /
    • pp.252-257
    • /
    • 2007
  • Escherichia coli HslVU is an ATP-dependent protease consisting of two heat shock proteins, the HslU ATPase and HslV peptidase. In the reconstituted enzyme, HslU stimulates the proteolytic activity of HslV by one to two orders of magnitude, while HslV increases the rate of ATP hydrolysis by HslU several-fold. Here we show that HslV alone can efficiently degrade certain unfolded proteins, such as unfolded lactalbumin and lysozyme prepared by complete reduction of disulfide bonds, but not their native forms. Furthermore, HslV alone cleaved a lactalbumin fragment sandwiched by two thioredoxin molecules, indicating that it can hydrolyze the internal peptide bonds of lactalbumin. Surprisingly, ATP inhibited the degradation of unfolded proteins by HslV. This inhibitory effect of ATP was markedly diminished by substitution of the Arg86 residue located in the apical pore of HslV with Gly, suggesting that interaction of ATP with the Arg residue blocks access of unfolded proteins to the proteolytic chamber of HslV. These results suggest that uncomplexed HslV is inactive under normal conditions, but may can degrade unfolded proteins when the ATP level is low, as it is during carbon starvation.

Up-regulation of Early Growth Response-1 Expression by Endoplasmic Reticulum Stress

  • ;;;;권오유
    • 대한의생명과학회지
    • /
    • 제13권2호
    • /
    • pp.157-160
    • /
    • 2007
  • Endoplasmic reticulum (ER) plays formation of disulfide bonds and proper folding of secretory proteins. Cellular responses to ER stress enhances the stress-activated kinase pathway and the induces a lot of immediate-early genes. Among of them, the early growth response-1 (Egr-1), a transcription factor, which plays an important role in cell growth, development, differentiation, apoptosis and various types of injury. For that reason, we have tested the expression of Egr-1 against ER stress inducible drugs (tunicamycin, DTT, A23187 and BFA) to understand what kind of aspect occurred by ER stresses.

  • PDF

Validation of Heterodimeric TAT-NLS Peptide as a Gene Delivery Enhancer

  • Doh, Kyung-Oh
    • Journal of Microbiology and Biotechnology
    • /
    • 제25권6호
    • /
    • pp.788-794
    • /
    • 2015
  • Cationic liposomes have been actively used as gene delivery vehicles despite their unsatisfactory efficiencies because of their relatively low toxicity. In this study, we designed novel heterodimeric peptides as nonviral gene delivery systems from TAT and NLS peptides using cysteine-to-cysteine disulfide bonds between the two. Mixing these heterodimeric peptides with DNA before mixing with lipofectamine resulted in higher transfection efficiencies in MCF-7 breast cancer cells than mixing unmodified TAT, NLS, and a simple mixture of TAT and NLS with DNA, but did not show an adverse effect on cell viability. In gel retardation assays, the DNA binding affinities of heterodimeric peptides were stronger than NLS but weaker than TAT. However, this enhancement was only observed when heterodimeric peptides were premixed with DNA before being mixed with lipofectamine. The described novel transfection-enhancing peptide system produced by the heterodimerization of TAT and NLS peptides followed by simple mixing with DNA, increased the gene transfer efficiency of cationic lipids without enhancing cytotoxicity.

Solution Structure of Human Orexin-A: Regulator of Appetite and Wakefulness

  • Kim, Hai-Young;Hong, Eun-Mi;Kim, Jae-Il;Lee, Weon-Tae
    • BMB Reports
    • /
    • 제37권5호
    • /
    • pp.565-573
    • /
    • 2004
  • Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are important hypothalamic neuro-peptides, which are encoded by a single mRNA transcript and stimulate food intake as well as regulate wakefulness. Here we determined the solution structure of orexin-A by NMR spectroscopy and by simulated-annealing calculation. The structural features of orexin-A involve two $\alpha$-helices, with the hydrophobic residues disposed to on one side of helix, and hydrophilic residues to the other. A hydrophilic turn induced by two disulfide bonds provides the key difference between orexin-A and -B. With previous mutagenic studies, the derived structure of orexin-A provides us with a structure-functional view for novel drug design.

Elctrophoretic Properties of Heat-Induced Bovine α-Lactalbumin

  • Lee, You-Ra;Hong, Youn-Ho
    • Preventive Nutrition and Food Science
    • /
    • 제7권1호
    • /
    • pp.48-51
    • /
    • 2002
  • In order to study the reaction behavior of bovine holo- and apo-$\alpha$-lactalbumin ($\alpha$-La) during heat treatment at 65~10$0^{\circ}C$, the samples were analysed by first (ID)-and second-dimensional (2D) native-polyacrylamide gel electrophoresis (Native-PAGE) and sodium dodecylsulfate (SDS)-PAGE. When bolo-$\alpha$-La or apo- $\alpha$ -La were heated, they formed non-native, monomers, dimers and trimers. The apo-$\alpha$-La was more heat-sensitive than holo-$\alpha$-La. The monomers seemed to have the same composition as the native $\alpha$-La, but many of the disulfide bonds could be non-native.