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Biological evaluation of Tyr6 and Ser7 modified drosocin analogues

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Author: Visser, P.C. de · Hooft, P.A.V. van · Vries, A.-M. de · Jong, A. de · Marel, G.A. van der · Overkleeft, H.S. · Noort, D.
Type:article
Date:2005
Institution: TNO Defensie en Veiligheid
Source:Bioorganic and Medicinal Chemistry Letters, 11, 15, 2902-2905
Identifier: 238547
doi: doi:10.1016/j.bmcl.2005.03.074
Keywords: Antibiotic agent · Amino acid substitution · Amino terminal sequence · Article · Controlled study · Drug screening · Drug stability · Drug synthesis · Nonhuman · Protein degradation · Amino Acid Sequence · Glycopeptides · Humans · Microbial Sensitivity Tests · Molecular Sequence Data · Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization · Chemicals · Drosocin, 179048-25-0 · Serine, 56-45-1, 6898-95-9 · Tyrosine, 16870-43-2, 55520-40-6, 60-18-4 · Drosocin, 149924-99-2 · Glycopeptides · Serine, 56-45-1 · Tyrosine, 55520-40-6

Abstract

An array of analogues of the cationic antimicrobial peptide drosocin was synthesized containing substitutions of Tyr6 and Ser7 in order to increase the proteolytic stability. Stabilizing the N-terminus with unnatural amino acids increased the serum stability of analogues by almost a factor 30 over an 8 h period. © 2005 Elsevier Ltd. All rights reserved.