Conformational Studies on Potential β‐Turn‐Forming Model Peptides

Bode, K.; Goodman, Murray; Mutter, Manfred

doi:10.1002/hlca.19850680320

Cited by 16 publications

(4 citation statements)

References 36 publications

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“…2. The spectrum is characterized by a negative Cotton effect at 230 nm and a strong positive band at about 200 nm which is typical for peptides adopting a @-turn conformation [22]. In contrast, the spectrum of I1 (not shown) is dominated by a strong negative Cotton effect at 200 nm accompanied by a weak minimum at 220 nm indicating a predominantly unordered conformation of I1 in Concerning the curve shape, the spectrum is very similar to that in CF,CH,OH, the negative Cotton effect being slightly blue-shifted to 224 nm.…”

Section: H-glu-(0bu')-gly-his-pro-gly-ser-(bu')-gly-pegm (11)mentioning

confidence: 99%

“…For this purpose, we decided to incorporate His, Ser, and Glu into a peptide sequence with a high potential to form a p-turn conformation [19]; Asp was replaced by Glu for synthetic reasons. Pro and Gly were chosen for the central positions i + 1 and i + 2 of the p-turn as suggested by empirical prediction schemes [20] [2 I ] and experimental investigations of model peptides [22] [23]. On the other hand, statistical analysis of globular proteins shows a high frequency of occurrence of His and Ser in turn positions i and i + 3, respectively [20].…”

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confidence: 99%

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Single‐Centre Model for the Active Site of α‐Chymotrypsin

Vorherr

Altmann

Mutter

1986

Helvetica Chimica Acta

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Dedicated to Prof. Rot/ C. Scliulz on the occasion of his 65Ih birthday (2O.Xl.85) The polymer-bound heptapeptide H-Glo-Gly-His-Pro-Gly-Ser-Gly-PEGM was designed as a 'single-centre model' for the active site of cc-chymotrypsin. The peptide was synthesized according to the general principles of the liquid-phase method for peptide synthesis, and its conformational properties were investigated by CD and IR spectroscopy in solution and in the solid state. In harmony with empirical prediction codes, experimental and theoretical conformational considerations, the peptide adopts a /&turn conformation stabilized by H-bonds involving the side chains of Glu, His, and Ser. The development of a H-bonded system similar to the active site of cc-chymotrypsin leads to implications with respect to a possible catalytic activity of the model peptide.Introduction. -In the last years, much work has been devoted to the construction of model systems imitating the unique catalytic properties of enzymes [ 1-31. The accessibility of such synthetic enzymes ('synzymes') would provide a valuable tool in organic synthesis to overcome some of the limiting shortcomings in the use of natural enzymes, e.g. problems of stability and solubility. Furthermore, the study of these simple models contributes to a better understanding of the mechanism of enzyme activity.Many attempts have been made to mimic the active site of a-Cht') [4-71, one of the most extensively studied proteolytic enzymes [8] [9]. Functionalized polymers and polypeptides have been studied for mimicing enzyme activity [10][11][12][13][14][15]; however, the lack of structural order in these systems proved to be a serious limitation in the interpretation and evaluation of the models [ 161.In a previous paper [I 71, we have described a 'single-centre model' as an approach for the elucidation of individual parameters contributing to enzyme-like activity. The model is based on amphiphilic block copolymers comprising a hydrophobic peptide block (containing a catalytically active group) and a hydrophilic PEG') block. Due to its strongly solubilizing effect, the PEG chain enables the investigation of otherwise insoluble peptide sequences even in aqueous solution without exerting a significant influence on the conformation of the peptide block [18].In the present paper, we wish to report about the design and conformational properties of a PEG-peptide serving as a single-centre model for the active site of cc-Cht.

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Section: H-glu-(0bu')-gly-his-pro-gly-ser-(bu')-gly-pegm (11)mentioning

confidence: 99%

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confidence: 99%

Single‐Centre Model for the Active Site of α‐Chymotrypsin

Vorherr

Altmann

Mutter

1986

Helvetica Chimica Acta

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“…These β-turn structures furnish a suitable model for investigating the short-range interactions between the side chain and the backbone, which play an important role in the aggregation process of proteins. − A number of conformational studies of short peptides, as models of a β-turn, have so far been carried out. − However, further studies of the property of this β-turn structure are highly desirable, to elucidate the role of the short-range interactions in proteins.…”

Section: Introductionmentioning

confidence: 99%

Folded Structures of l-Leucylglycine Oligopeptides and Their Aggregational Behavior in Aqueous Solution: Raman Scattering Spectra and Proton NMR Spin−Lattice Relaxation Studies

et al. 2008

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The aggregational behavior of three L-leucylglycine oligopeptides (residue numbers of glycine are 3, 4, and 5) in aqueous solution was investigated by the use of Raman scattering and 1H NMR spin-lattice relaxation methods. The results indicate that their oligopeptides take up a folded structure to form dimeric aggregates above their critical aggregation concentration. The application of one-dimensional aggregate theory to these systems provides the following prediction. Elongation up to 6 glycine residues makes it possible to form dimeric aggregates, but further elongation (up to 7 glycine residues) makes the aggregates very unstable, and up to 8 or 9 glycine residues makes the formation of dimeric aggregates very difficult. The one-dimensional aggregate theory may be used to predict the existence of peptide aggregates through intermolecular hydrogen bonding.

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“…As an appropriate tribute to M. Goodman's memory and to two different areas of peptide chemistry and stereochemistry (β‐turn conformation3–5 and C α ‐methylated α‐amino acids) where he was also active,6, 7 we present here our crystal‐state three‐dimensional (3D) structural characterization by X‐ray diffraction of eight N α ‐acylated short peptides (from trimers to a pentamer), but long enough to form a β‐turn conformation. All peptides are rich in the β‐turn stabilizing C α ‐methylated α‐amino acids 8–12.…”

Section: Introductionmentioning

confidence: 99%

Turn stabilization in short peptides by C^α‐methylated α‐amino acids

et al. 2004

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Abstract:The crystal-state conformations of three protected tripeptides, four tetrapeptides, and one pentapeptide, heavily based on the chiral C ␣ -methylated ␣-amino acids Iva, (␣Me)Nva, and (Me)Val, were assessed by X-ray diffraction analyses. The eight peptide sequences are as follows: and Z-L-Ala-[L-(␣Me)Nva] 4 -OtBu. Two independent molecules were observed in the asymmetric units of Z-D-Iva-L-Iva-Gly-OtBu and Z-Aib-[L-(␣Me)Nva] 2 -OtBu, while three independent molecules were seen in Z-L-Ala-[L-(␣Me)Nva] 4 -OtBu. All peptides are folded in a single or multiple ␤-turn conformations. Interestingly: (i) a water bridge within the N-terminal

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Conformational Studies on Potential β‐Turn‐Forming Model Peptides

Cited by 16 publications

References 36 publications

Single‐Centre Model for the Active Site of α‐Chymotrypsin

Single‐Centre Model for the Active Site of α‐Chymotrypsin

Folded Structures of l-Leucylglycine Oligopeptides and Their Aggregational Behavior in Aqueous Solution: Raman Scattering Spectra and Proton NMR Spin−Lattice Relaxation Studies

Turn stabilization in short peptides by C^α‐methylated α‐amino acids

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Conformational Studies on Potential β‐Turn‐Forming Model Peptides

Cited by 16 publications

References 36 publications

Single‐Centre Model for the Active Site of α‐Chymotrypsin

Single‐Centre Model for the Active Site of α‐Chymotrypsin

Folded Structures of l-Leucylglycine Oligopeptides and Their Aggregational Behavior in Aqueous Solution: Raman Scattering Spectra and Proton NMR Spin−Lattice Relaxation Studies

Turn stabilization in short peptides by Cα‐methylated α‐amino acids

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Turn stabilization in short peptides by C^α‐methylated α‐amino acids