Polymer-supported biopolymer synthesis: 4. Synthesis of dynorphin (1–13) by condensation of protected peptide segments prepared by high-load solid (gel) phase methods

Small, P.W.; Epton, R.; Marr, G.; Twaij, Saleh

doi:10.1016/0141-8130(84)90029-1

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International Journal of Biological Macromolecules

1984

DOI: 10.1016/0141-8130(84)90029-1

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Polymer-supported biopolymer synthesis: 4. Synthesis of dynorphin (1–13) by condensation of protected peptide segments prepared by high-load solid (gel) phase methods

P.W. Small

R. Epton

G. Marr

et al.

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1993

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Cited by 3 publications

References 14 publications

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Polymer-supported biopolymer synthesis: 5. Ultra-high load solid (gel) phase peptide synthesis—the stepwise elaboration of quasi-homogeneous peptide gel networks?

Epton

Marr

McGinn

et al. 1985

International Journal of Biological Macromolecules

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Polymer-supported biopolymer synthesis: 5. Ultra-high load solid (gel) phase peptide synthesis—the stepwise elaboration of quasi-homogeneous peptide gel networks?

Epton

Marr

McGinn

et al. 1985

International Journal of Biological Macromolecules

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Convergent solid-phase peptide synthesis

1993

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Tryptophan reduction and histidine racemization during deprotection by catalytic transfer hydrogenation of an analog of the luteinizing hormone releasing factor

Méry¹,

Calas²

1988

International Journal of Peptide and Protein Research

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(d‐Trp)6‐LHRH:pGlu‐His‐Trp‐Ser‐Tyr‐d‐Trp‐Leu‐Arg‐Pro‐GlyNH2 was prepared by solid‐phase peptide synthesis using the nitro group to protect the guanidine side chain of the arginyl residue. Removal of the side‐chain protecting groups was carried out by catalytic transfer hydrogenation (CTH) using palladium acetate/ammonium formate or palladium on charcoal/formic acid. We show in this paper that this deprotection method induces i) reduction of the tryptophan residue and ii) epimerization at the histidine level (with palladium acetate/ammonium formate). Despite the formation of significant amounts of reduced peptide. CTH enabled us to obtain (d‐Trp)6‐LHRH in relatively good yield.

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Polymer-supported biopolymer synthesis: 4. Synthesis of dynorphin (1–13) by condensation of protected peptide segments prepared by high-load solid (gel) phase methods

Cited by 3 publications

References 14 publications

Polymer-supported biopolymer synthesis: 5. Ultra-high load solid (gel) phase peptide synthesis—the stepwise elaboration of quasi-homogeneous peptide gel networks?

Polymer-supported biopolymer synthesis: 5. Ultra-high load solid (gel) phase peptide synthesis—the stepwise elaboration of quasi-homogeneous peptide gel networks?

Convergent solid-phase peptide synthesis

Tryptophan reduction and histidine racemization during deprotection by catalytic transfer hydrogenation of an analog of the luteinizing hormone releasing factor

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