1996
DOI: 10.1039/cc9960002089
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Intermolecular stabilisation of the β-sheet conformation in dipeptides

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Cited by 39 publications
(22 citation statements)
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“…[21] A logical extension affords the first soluble β-sheet models, in which combinations of these artificial (Nowick [22] ) and natural (Kemp, [23] Feigel, [24] Kelly, [25] Gellman [26] ) peptide strands are attached to common scaffolds and interact along their inner faces like zippers to form two-or three-stranded parallel or antiparallel β-sheets. Very recently the first intermolecular versions of these β-sheet models were created (Schrader, [27] Hamil-ton, [28] Bartlett [29] ), albeit in organic solvents. Aminopyrazoles, diaminoquinolones and azacyclohexenones ( Figure 2) are thus all able to form the maximum number of possible hydrogen bonds to the top and bottom faces of an extended peptide strand backbone.…”
Section: Introductionmentioning
confidence: 99%
“…[21] A logical extension affords the first soluble β-sheet models, in which combinations of these artificial (Nowick [22] ) and natural (Kemp, [23] Feigel, [24] Kelly, [25] Gellman [26] ) peptide strands are attached to common scaffolds and interact along their inner faces like zippers to form two-or three-stranded parallel or antiparallel β-sheets. Very recently the first intermolecular versions of these β-sheet models were created (Schrader, [27] Hamil-ton, [28] Bartlett [29] ), albeit in organic solvents. Aminopyrazoles, diaminoquinolones and azacyclohexenones ( Figure 2) are thus all able to form the maximum number of possible hydrogen bonds to the top and bottom faces of an extended peptide strand backbone.…”
Section: Introductionmentioning
confidence: 99%
“…These rigid heterocyclic structures have been investigated in solution with respect to their backbone recognition abilities by various NMR and IR spectroscopic methods as well as by force-field calculations. [4][5][6][7][8] To successfully compete with peptide dimerization, such a ligand must form a peptide complex with a superior gain of free enthalpy. Many different factors, however, determine its overall affinity in solution, among others solvation energies and secondary structure stabilities of the peptide environment.…”
mentioning
confidence: 99%
“…Simple ␤-sheet templates have also been incorporated into drugs that bind to a peptide region with ␤-sheet conformation (34). However, external templates, which force a peptide strand into the ␤-sheet conformation, are very rare (35)(36)(37). Meredith and co-workers (26,27) very recently demonstrated the paramount importance of backbone hydrogen bonding for the formation of ␤-amyloid fibrils; replacing the amide bonds by ester linkages completely eliminated any aggregation propensity of the respective peptide-like compound taken from the A␤ sequence (26,27).…”
Section: Concept Andmentioning
confidence: 99%