Synthesis of cyclic peptides via efficient new coupling reagents

Ehrlich, Angelika; Rothemund, Sven; Brudel, M.; Beyermann, Michael; Carpino, Louis A.; Bienert, Michael

doi:10.1007/978-94-011-0683-2_26

Cited by 7 publications

(9 citation statements)

References 4 publications

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“…So both for synthesis, and to stabilize β-turns, a favourable structure should contain at least one Gly, Pro or D-residue. Further proof of the advantages of a D-residue was obtained in the cyclization [99] of a thymopentin analogue. Using BOP and other HOBt reagents on H-ValArg-Lys(Ac)-Ala-Val-Tyr-OH did achieve up to 25% cyclization but extensive racemization of the Tyr residue took place.…”

Section: Cyclotripeptides All-l Cyclotripeptides With All α-mentioning

confidence: 97%

The cyclization of peptides and depsipeptides

Davies

2003

Journal of Peptide Science

413

241

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Constricting the peptide backbone into a more defined conformational form through cyclization is an activity evolved in nature and in synthetic work, the latter straddling only the most recent decades. The resulting conformational constraints increase the probability of an optimum response with bio-receptors. The purpose of this review is to highlight developments that have proved to be reasonably efficient in the macrocyclization of linear precursors into cyclic peptides and depsipeptides.

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Section: Cyclotripeptides All-l Cyclotripeptides With All α-mentioning

confidence: 97%

The cyclization of peptides and depsipeptides

Davies

2003

Journal of Peptide Science

413

241

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“…All linear peptides were synthesized manually by the solid‐phase method using standard Fmoc strategy (29, 30). Head‐to‐tail cyclization of linear precursor peptides was performed by HAPyU chemistry (31, 32). The peptides were purified by preparative reversed phase (RP)‐HPLC and purity of all peptides was found to be >95% by HPLC analysis.…”

Section: Peptide Synthesis and Characterizationmentioning

confidence: 99%

Antimicrobial activity of arginine‐ and tryptophan‐rich hexapeptides: the effects of aromatic clusters, d‐amino acid substitution and cyclization

Wessolowski¹,

Bienert²,

Dathe³

2004

The Journal of Peptide Research

Self Cite

112

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Many antimicrobial peptides bear arginine (R)- and tryptophan (W)-rich sequence motifs. Based on the sequence Ac-RRWWRF-NH2, sets of linear and cyclic peptides were generated by changes in the amino acid sequence, L-D-amino acid exchange and naphthylalanine substituted for tryptophan. Linear RW-peptides displayed moderate activity towards Gram-positive Bacillus subtilis (15 < MIC < 31 microm) and were inactive against Gram-negative Escherichia coli at peptide concentrations < 100 microm. Cyclization induced high antimicrobial activity. The effect of cyclization was most pronounced for peptides with three adjacent aromatic residues. Incorporation of d-amino acid residues had minor influence on the biological activity. The haemolytic activity of all RW-peptides at 100 microm concentration was low (< 7% lysis for linear R/W-rich peptides and < 28% for the cyclic analogues). Introduction of naphthylalanine enhanced the biological activities of both the linear and cyclic peptides. All peptides induced permeabilization of large unilamellar vesicles (LUVs) composed of lipids of the membrane of B. subtilis and erythrocytes, but surprisingly had no effect on LUVs composed of lipids of the E. coli inner membrane. The profiles of peptide activity against B. subtilis and red blood cells correlated with the permeabilizing effects on the corresponding model membranes and were related to hydrophobicity parameters as derived from reversed phase high-performance liquid chromatography (HPLC). The results underlined the importance of amphipathicity as a driving force for cell lytic activity and suggest that conformational constraints and an appropriate position of aromatic residues allowing the formation of hydrophobic clusters are highly favourable for antimicrobial activity and selectivity.

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“…Usually, no difficulties arise from the cyclization of free linear peptides containing seven or more amino acid residues [12]. However, the cyclization of pentapeptides is often difficult because cyclodimerization to a Copyright cyclodecapeptide can occur easily [13,14]. An effective method to prevent cyclodimerization is to close the linear peptide precursor in highly dilute solutions (10 −3 -10 −4 M) [15,16].…”

Section: Introductionmentioning

confidence: 99%

Studies on the synthesis of cyclic pentapeptides as LHRH antagonists and the factors that influence cyclization yield

Gao

Bernd³

et al. 2002

Journal of Peptide Science

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Six cyclic pentapeptides containing two or three non-protein amino acids have been synthesized by cyclization of linear precursors in dilute solution and characterized by TLC. HPLC, NMR, melting point. specific rotation etc. A total of 72 cyclization reactions were carried out to study the factors that influence head-to-tail cyclization: linear precursor sequence, coupling reagent, residue configuration, the proportion of DMAP additive, concentration, reaction temperature and reaction time. The cyclic pentapeptides will be modified by active moieties and evaluated as LHRH antagonists.

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Synthesis of cyclic peptides via efficient new coupling reagents

Cited by 7 publications

References 4 publications

The cyclization of peptides and depsipeptides

The cyclization of peptides and depsipeptides

Antimicrobial activity of arginine‐ and tryptophan‐rich hexapeptides: the effects of aromatic clusters, d‐amino acid substitution and cyclization

Studies on the synthesis of cyclic pentapeptides as LHRH antagonists and the factors that influence cyclization yield

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