All-D-magainin: chirality, antimicrobial activity and proteolytic resistance

Roberto Bessalle; Aviva Kapitkovsky; Alfred Gorea; Itamar Shalit; Mati Fridkin

doi:10.1016/0014-5793(90)81351-N

All-D-magainin: chirality, antimicrobial activity and proteolytic resistance

Roberto Bessalle
, Aviva Kapitkovsky
, Alfred Gorea
, Itamar Shalit
, Mati Fridkin^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

318 Scopus citations

Abstract

All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic α -helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.

Original language	English
Pages (from-to)	151-155
Number of pages	5
Journal	FEBS Letters
Volume	274
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)81351-N
State	Published - 12 Nov 1990
Externally published	Yes

Keywords

All-D-magainin
Proteolytic stability: Clinical potential
Surface-activity

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10.1016/0014-5793(90)81351-N

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abstract = "All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic α -helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.",

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AU - Shalit, Itamar

AU - Fridkin, Mati

PY - 1990/11/12

Y1 - 1990/11/12

N2 - All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic α -helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.

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KW - All-D-magainin

KW - Proteolytic stability: Clinical potential

KW - Surface-activity

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All-D-magainin: chirality, antimicrobial activity and proteolytic resistance

Abstract

Keywords

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