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• W1999465043 endingPage "1427" @default.
• W1999465043 startingPage "1418" @default.
• W1999465043 abstract "Unlike α-amino acids, peptides formed from β-amino acids (β-peptides) display stability toward enzymatic degradation and may form turns and helices with as few as four residues. Because both the Cα and Cβ of the β-amino acid may bear substituents, a large number of β-amino acids can be synthesized. β-Peptides form various well-defined secondary structures, including 14-helix, 12-helix, 10/12-helix, 10-helix, 8-helix, turn structures, sheets, and hairpins. For all of these reasons, β-amino acids have been increasingly used as building blocks for molecular design and pharmaceutical applications. To explain the conformational features of β-peptides, several quantum mechanics and molecular dynamics studies that rationalize the observed conformational features have been reported. However, a systematic account that unifies various factors critical to the conformational features is still lacking. In this Account, we present a detailed analysis of the conformational features of various β-peptides. We start by studying the basic local conformational features of β-peptides using di- and tripeptide models. Then, various secondary structures of unsubstituted β-peptides with differing numbers of residues are investigated using a repeating unit approach to derive the intrinsic backbone conformational features. We find that the 10/12-helix is intrinsically most stable for the β-peptide backbone. The 14-helix, 12-helix, and 10-helix structures have similar stabilities for β-peptide backbones of four to six residues. The substituent effects on the stabilities of β-peptide secondary structures are then analyzed. Combined with the substituent effect and the intrinsic backbone preferences, all experimental observations of secondary structure formation can be understood. For example, the 10/12-helix is favored for like-β2/β3-peptides, unlike-β3/β3-peptides, and β3/β-hGly-peptides because these substitution patterns do not cause steric problems for the 10/12-helix. β3-Peptides, β2-peptides, and β2,3-peptides favor the 14-helix because the substituents in these peptides benefit the 14-helix the most but significantly destabilize the 10/12-helix. Because the 10/12-helix is intrinsically favored and has two favorable positions in each residue for substituents, many more hybrid β-peptides are predicted to exist in this secondary structure, which suggests the need for further experiments. These results are valuable for determining the best use of these building blocks in the design of well-structured molecules with desirable chemical functions." @default.
• W1999465043 created "2016-06-24" @default.
• W1999465043 creator A5014043910 @default.
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• W1999465043 creator A5079289838 @default.
• W1999465043 creator A5080751870 @default.
• W1999465043 creator A5091183669 @default.
• W1999465043 date "2008-10-02" @default.
• W1999465043 modified "2023-10-11" @default.
• W1999465043 title "Theoretical Analysis of Secondary Structures of β-Peptides" @default.
• W1999465043 cites W1491552426 @default.
• W1999465043 cites W1501359805 @default.
• W1999465043 cites W1566352095 @default.
• W1999465043 cites W1874698966 @default.
• W1999465043 cites W1971636489 @default.
• W1999465043 cites W1973535048 @default.
• W1999465043 cites W1973646267 @default.
• W1999465043 cites W1974070925 @default.
• W1999465043 cites W1975313075 @default.
• W1999465043 cites W1979737039 @default.
• W1999465043 cites W1981989090 @default.
• W1999465043 cites W1982845463 @default.
• W1999465043 cites W1983772763 @default.
• W1999465043 cites W1985974805 @default.
• W1999465043 cites W1986447658 @default.
• W1999465043 cites W1990437549 @default.
• W1999465043 cites W1991877201 @default.
• W1999465043 cites W1992534603 @default.
• W1999465043 cites W1994349900 @default.
• W1999465043 cites W1995056314 @default.
• W1999465043 cites W2000505028 @default.
• W1999465043 cites W2002021814 @default.
• W1999465043 cites W2005181751 @default.
• W1999465043 cites W2008424351 @default.
• W1999465043 cites W2008583771 @default.
• W1999465043 cites W2010087060 @default.
• W1999465043 cites W2017598128 @default.
• W1999465043 cites W2018717750 @default.
• W1999465043 cites W2021198082 @default.
• W1999465043 cites W2021876920 @default.
• W1999465043 cites W2022354406 @default.
• W1999465043 cites W2024935501 @default.
• W1999465043 cites W2024947155 @default.
• W1999465043 cites W2028530561 @default.
• W1999465043 cites W2028760518 @default.
• W1999465043 cites W2030214692 @default.
• W1999465043 cites W2033103812 @default.
• W1999465043 cites W2037498259 @default.
• W1999465043 cites W2037780945 @default.
• W1999465043 cites W2038602336 @default.
• W1999465043 cites W2039421829 @default.
• W1999465043 cites W2045878175 @default.
• W1999465043 cites W2052252427 @default.
• W1999465043 cites W2054808758 @default.
• W1999465043 cites W2058550326 @default.
• W1999465043 cites W2058933525 @default.
• W1999465043 cites W2064053933 @default.
• W1999465043 cites W2064864164 @default.
• W1999465043 cites W2066414077 @default.
• W1999465043 cites W2066842297 @default.
• W1999465043 cites W2070421067 @default.
• W1999465043 cites W2071373488 @default.
• W1999465043 cites W2073714801 @default.
• W1999465043 cites W2079508576 @default.
• W1999465043 cites W2084017179 @default.
• W1999465043 cites W2085915211 @default.
• W1999465043 cites W2089549170 @default.
• W1999465043 cites W2090514011 @default.
• W1999465043 cites W2094446407 @default.
• W1999465043 cites W2096649736 @default.
• W1999465043 cites W2097791955 @default.
• W1999465043 cites W2102291985 @default.
• W1999465043 cites W2103902008 @default.
• W1999465043 cites W2105896488 @default.
• W1999465043 cites W2109080201 @default.
• W1999465043 cites W2112397081 @default.
• W1999465043 cites W2113301225 @default.
• W1999465043 cites W2115792147 @default.
• W1999465043 cites W2118905518 @default.
• W1999465043 cites W2130087627 @default.
• W1999465043 cites W2132762304 @default.
• W1999465043 cites W2133340957 @default.
• W1999465043 cites W2144642321 @default.
• W1999465043 cites W2155395547 @default.
• W1999465043 cites W2165779834 @default.
• W1999465043 cites W2177704805 @default.
• W1999465043 cites W2178092299 @default.
• W1999465043 cites W2310328055 @default.
• W1999465043 cites W4297193224 @default.
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• W1999465043 doi "https://doi.org/10.1021/ar800070b" @default.
• W1999465043 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18828608" @default.
• W1999465043 hasPublicationYear "2008" @default.
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