Effect of phospholipid bilayers on solution conformation of branched polymeric polypeptides and peptide-polymer conjugates

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6 Citations (Scopus)

Abstract

This report provides a detailed analysis on the influence of phosholipid bilayers on the conformation of poly[Lys(Xi-DL-Alam)] (XAK, where X = Ser, Orn, Glu, or AcGlu) type branched polypeptides and their peptide conjugates. CD spectra of polycationic (SAK, OAK), amphoteric (EAK), or polyanionic (Ac-EAK) polylysine derivatives were recorded in 0.25M acetate buffer at pH 7.4 as well as in the presence of DPPC or DPPC/PG (95/5, 80/20 mol/mol) liposomes. Based on these data, two groups of polypeptides are described. Group one contains polypeptides with significantly ordered conformation even in buffer solution (SAK, AcEAK), which is essentially not altered by phospholipids. Group two, branched polypeptides (OAK, EAK), with only partially ordered conformation in aqueous solution in the presence of phospholipid bilayers with high PG content, could adopt more (EAK) or less (OAK) ordered α-helical structure depending on their charge properties. In addition, we report on the synthesis of two new sets of oligopeptide-branched polypeptide conjugates. Studies with selected conjugates suggest that these compounds are highly ordered in buffer solution almost regardless from the helix-forming ability of the carrier (AK, SAK, EAK) and from the hydrophilic/hydrophobic character of peptides attached (AVKDEL vs FWRGDLVFDFQV). Addition of phospholipid bilayers with different composition essentially had no modifying effect on conformation of conjugates. From this we can conclude that the covalently coupled oligopeptides has a predominant effect of the conformational properties of conjugates.

Original languageEnglish
Pages (from-to)152-164
Number of pages13
JournalBiopolymers - Peptide Science Section
Volume58
Issue number2
DOIs
Publication statusPublished - 2001

Fingerprint

Polypeptides
Phospholipids
Peptides
Conformations
Polymers
Oligopeptides
Buffers
Liposomes
Polylysine
Acetates
Derivatives
Chemical analysis

Keywords

  • Branched chain synthetic polypeptides
  • CD spectroscopy of synthetic polypeptides
  • Drug/epitope targeting and delivery
  • Liposomes membrane
  • Macromolecular carriers
  • Membrane-peptide-conjugate interaction
  • Membrane-polypeptide interaction
  • Phospholipid membrane models of DPPC and PG

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

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title = "Effect of phospholipid bilayers on solution conformation of branched polymeric polypeptides and peptide-polymer conjugates",
abstract = "This report provides a detailed analysis on the influence of phosholipid bilayers on the conformation of poly[Lys(Xi-DL-Alam)] (XAK, where X = Ser, Orn, Glu, or AcGlu) type branched polypeptides and their peptide conjugates. CD spectra of polycationic (SAK, OAK), amphoteric (EAK), or polyanionic (Ac-EAK) polylysine derivatives were recorded in 0.25M acetate buffer at pH 7.4 as well as in the presence of DPPC or DPPC/PG (95/5, 80/20 mol/mol) liposomes. Based on these data, two groups of polypeptides are described. Group one contains polypeptides with significantly ordered conformation even in buffer solution (SAK, AcEAK), which is essentially not altered by phospholipids. Group two, branched polypeptides (OAK, EAK), with only partially ordered conformation in aqueous solution in the presence of phospholipid bilayers with high PG content, could adopt more (EAK) or less (OAK) ordered α-helical structure depending on their charge properties. In addition, we report on the synthesis of two new sets of oligopeptide-branched polypeptide conjugates. Studies with selected conjugates suggest that these compounds are highly ordered in buffer solution almost regardless from the helix-forming ability of the carrier (AK, SAK, EAK) and from the hydrophilic/hydrophobic character of peptides attached (AVKDEL vs FWRGDLVFDFQV). Addition of phospholipid bilayers with different composition essentially had no modifying effect on conformation of conjugates. From this we can conclude that the covalently coupled oligopeptides has a predominant effect of the conformational properties of conjugates.",
keywords = "Branched chain synthetic polypeptides, CD spectroscopy of synthetic polypeptides, Drug/epitope targeting and delivery, Liposomes membrane, Macromolecular carriers, Membrane-peptide-conjugate interaction, Membrane-polypeptide interaction, Phospholipid membrane models of DPPC and PG",
author = "I. Nagy and Zs. Majer and F. Hudecz",
year = "2001",
doi = "10.1002/1097-0282(200102)58:2<152::AID-BIP40>3.0.CO;2-V",
language = "English",
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T1 - Effect of phospholipid bilayers on solution conformation of branched polymeric polypeptides and peptide-polymer conjugates

AU - Nagy, I.

AU - Majer, Zs.

AU - Hudecz, F.

PY - 2001

Y1 - 2001

N2 - This report provides a detailed analysis on the influence of phosholipid bilayers on the conformation of poly[Lys(Xi-DL-Alam)] (XAK, where X = Ser, Orn, Glu, or AcGlu) type branched polypeptides and their peptide conjugates. CD spectra of polycationic (SAK, OAK), amphoteric (EAK), or polyanionic (Ac-EAK) polylysine derivatives were recorded in 0.25M acetate buffer at pH 7.4 as well as in the presence of DPPC or DPPC/PG (95/5, 80/20 mol/mol) liposomes. Based on these data, two groups of polypeptides are described. Group one contains polypeptides with significantly ordered conformation even in buffer solution (SAK, AcEAK), which is essentially not altered by phospholipids. Group two, branched polypeptides (OAK, EAK), with only partially ordered conformation in aqueous solution in the presence of phospholipid bilayers with high PG content, could adopt more (EAK) or less (OAK) ordered α-helical structure depending on their charge properties. In addition, we report on the synthesis of two new sets of oligopeptide-branched polypeptide conjugates. Studies with selected conjugates suggest that these compounds are highly ordered in buffer solution almost regardless from the helix-forming ability of the carrier (AK, SAK, EAK) and from the hydrophilic/hydrophobic character of peptides attached (AVKDEL vs FWRGDLVFDFQV). Addition of phospholipid bilayers with different composition essentially had no modifying effect on conformation of conjugates. From this we can conclude that the covalently coupled oligopeptides has a predominant effect of the conformational properties of conjugates.

AB - This report provides a detailed analysis on the influence of phosholipid bilayers on the conformation of poly[Lys(Xi-DL-Alam)] (XAK, where X = Ser, Orn, Glu, or AcGlu) type branched polypeptides and their peptide conjugates. CD spectra of polycationic (SAK, OAK), amphoteric (EAK), or polyanionic (Ac-EAK) polylysine derivatives were recorded in 0.25M acetate buffer at pH 7.4 as well as in the presence of DPPC or DPPC/PG (95/5, 80/20 mol/mol) liposomes. Based on these data, two groups of polypeptides are described. Group one contains polypeptides with significantly ordered conformation even in buffer solution (SAK, AcEAK), which is essentially not altered by phospholipids. Group two, branched polypeptides (OAK, EAK), with only partially ordered conformation in aqueous solution in the presence of phospholipid bilayers with high PG content, could adopt more (EAK) or less (OAK) ordered α-helical structure depending on their charge properties. In addition, we report on the synthesis of two new sets of oligopeptide-branched polypeptide conjugates. Studies with selected conjugates suggest that these compounds are highly ordered in buffer solution almost regardless from the helix-forming ability of the carrier (AK, SAK, EAK) and from the hydrophilic/hydrophobic character of peptides attached (AVKDEL vs FWRGDLVFDFQV). Addition of phospholipid bilayers with different composition essentially had no modifying effect on conformation of conjugates. From this we can conclude that the covalently coupled oligopeptides has a predominant effect of the conformational properties of conjugates.

KW - Branched chain synthetic polypeptides

KW - CD spectroscopy of synthetic polypeptides

KW - Drug/epitope targeting and delivery

KW - Liposomes membrane

KW - Macromolecular carriers

KW - Membrane-peptide-conjugate interaction

KW - Membrane-polypeptide interaction

KW - Phospholipid membrane models of DPPC and PG

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U2 - 10.1002/1097-0282(200102)58:2<152::AID-BIP40>3.0.CO;2-V

DO - 10.1002/1097-0282(200102)58:2<152::AID-BIP40>3.0.CO;2-V

M3 - Article

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VL - 58

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SN - 0006-3525

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