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Synthetic S ‐(2,3‐dihydroxypropyl)‐cysteinyl peptides derived from the N‐terminus of the cytochrome subunit of the photoreaction centre of Rhodopseudomonas viridis enhance murine splenocyte proliferation
Author(s) -
Metzger Jörg W.,
BeckSickinger Annette G.,
Loeit Manuel,
Eckert Marianne,
Bessler Wolfgang G.,
Jung Günther
Publication year - 1995
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.310010305
Subject(s) - lipopeptide , chemistry , stereochemistry , rhodopseudomonas palustris , tetrapeptide , peptide , biochemistry , residue (chemistry) , splenocyte , amide , cytochrome c , biology , bacteria , in vitro , apoptosis , genetics
Various lipopeptides representing the N‐terminal part of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas virdis were prepared by solid‐phase peptide synthesis. These lipopeptides consisted of a S ‐[2,3‐dihydroxypropyl]‐cysteinyl (Dhc) residue N‐terminally coupled to the nonapeptide FEPPPATTT. Different numbers of palmitoyl (Pam) chains were attached to Dhc via ester and/or amide bonds. The lipopeptide Dhc(Pam) 2 ‐FEPPPATTT containing two ester‐bonded palmitoyl residues and a free N‐chain lipopeptide Pam‐Dhc(Pam)‐FEPPPATTT containing one amide‐ and one ester‐bonded palmitoyl residues, the two‐chain lipopeptide Pam‐Dhc(Pam)‐FEPPPATTT containing one amide‐ and one ester‐bonded palmitoyl residue, and the N‐terminally elongated lipopeptide SLVAG‐Dhc(Pam) 2 ‐FEPPPATTT were less active. The nonapeptide FEPPPATTT and the decapeptide Dhc‐FEPPPATTT were only merginal splenocyte activators, even at concentrations as high as 1 μ M . Thus, lipopeptide Dhc(Pam) 2 ‐FEPPPATTT constitutes the first potent splenocyte stimulating Dhc‐lipopeptide described so far that contains only two fatty acid residues.