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peptoids with aliphatic sidechains as helical structures without hydrogen bonds and collagen/ inverse-collagen type structures

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Journal of Biophysical Chemistry 2011年第1期2卷 37-48页

作者： Fateh S. Nandel Avneet Saini 不详

Aliphatic homo-polypeptoids of NAla, NVal, NIle and NLeu both in the presence and absence of protecting groups adopt helical structures without hydrogen bonds with Φ, Ψ values of ~ 0, ± 90° with trans amide bonds. These structures are stabilized by carbonyl-carbonyl interactions and characterized by ~ 3.16 residues per turn with a pitch of ~ 6.13 ?. It has been shown that like polyvaline and polyleucine peptides, poly-peptoids can also be exploited for the construction of potential surfactant like molecules by incorporating charged amino acid residues at the N terminal. A single-handed template with Φ, Ψ values of ~ 0, 90° can be attained by incorporating L-leu or L-val at the C-terminal of poly-NIle. Analysis of the simulation results in water as a function of time reveals that the opening of helical structures without hydrogen bonds takes place at sub-picosecond time scale starting from the N-terminal. This leads to the formation of collagen or inverse-collagen type structures (Φ, Ψ ~ -60, 145° and 60, -145° respectively) stabilized by interactions of water molecules with the backbone carbonyl groups.

关键词： peptoids Conformation Helical Structure without Hydrogen Bonds Collagen and Inverse-Collagen Type Structures

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Synthesis and biological evaluation of tetrahydroisoquinoline derivatives as potential multidrug resistance reversal agents in cancer

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Chinese Chemical Letters 2008年第2期19卷 169-171页

作者： Yu Li Hui Bin Zhang Wen Long Huang Xia Zhen Yun Man Li Center of Drug Discovery China Pharmaceutical University Nanjing 210009 China

Tetrahydroisoquinoline derivatives were synthesized and their multidrug resistance reversal activities were evaluated in vitro. The results showed that some of the synthetic compounds had higher multidrug resistance ... 详细信息

关键词： Tetrahydroisoquinoline derivatives Synthesis Mulfidrug resistance (MDR) peptoids

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Telechelic Triblock Poly(α-Amino Acid)-Poly(Tetrahydrofuran)-Poly(α-Amino Acid)Copolymers:Chain-End Transformation,Polymerization and pH-Responsive Hydrolysis

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Chinese Journal of Chemistry 2021年第10期39卷 2852-2856页

作者： Peng Zhou Zixian Li Yanzhi Lu Jie Kong Jun Ling MOE Key Laboratory of Macromolecular Synthesis and Functionalization Department of Polymer Science and EngineeringZhejiang UniversityHangzhouZhejiang310027 China Shaanxi Key Laboratory of Macromoleculor Science and Technology School of Chemistry and Chemical EngineeringNorthwestern Polytechnicol UniversityXi'onZhejiang 710072China

Main observation and conclusion Block copolymers not only combine properties of different segments but also generate new application ***(α-amino acid)-b-poly(tetrahydrofuran)-b-poly(α-amino acid)(PAA-PTHF-PAA)is one of the *** this contribution,di-hydroxyl-ended HO-PTHF-OH is transferred into di-oxyamino-ended H2NO-PTHF-ONH2 quantitatively,which is used as a macroinitiator to polymerize sarcosine N-thiocarboxyanhydride(Sar-NTA)and N-phenyoxycarbonyl N-ε-carbobenzyloxy-D-lysine(ZDL-NPC).Well-defined triblock PAA-NHO-PTHF-ONH-PAA is produced with high molecular weight(up to 25.3 kg/mol)and narrow *** amphiphilic PSar-NHO-PTHF-ONH-PSar(STS)self-assembles into micelles with uniform diameters of 30—40 nm according to *** to oxygen amide groups inside the backbone of these copolymers,the polyether-poly(amino acid)s block copolymers are cleavable under an acidic environment and therefore have potential applications in smart biomedicine and engineering.

关键词： End group transformation Block copolymers Amino acid Peptides peptoids

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