Secondary conformation of short lysine- and leucine-rich peptides assessed by optical spectroscopies: effect of chain length, concentration, solvent, and time.
Identifieur interne : 000193 ( France/Analysis ); précédent : 000192; suivant : 000194Secondary conformation of short lysine- and leucine-rich peptides assessed by optical spectroscopies: effect of chain length, concentration, solvent, and time.
Auteurs : Belén Hernández [France] ; F-Z Boukhalfa-Heniche ; Olivier Seksek ; Yves-Marie Coïc ; Mahmoud GhomiSource :
- Biopolymers [ 0006-3525 ] ; 2006.
Descripteurs français
- KwdFr :
- Analyse spectrale, Analyse spectrale Raman, Cinétique, Conformation des protéines, Dichroïsme circulaire, Données de séquences moléculaires, Leucine (), Lysine (), Méthanol (), Oligopeptides (), Oligopeptides (analyse), Peptides (), Peptides (analyse), Solvants (), Structure secondaire des protéines, Séquence d'acides aminés, Trométhamine ().
- MESH :
- analyse : Oligopeptides, Peptides.
- Analyse spectrale, Analyse spectrale Raman, Cinétique, Conformation des protéines, Dichroïsme circulaire, Données de séquences moléculaires, Leucine, Lysine, Méthanol, Oligopeptides, Peptides, Solvants, Structure secondaire des protéines, Séquence d'acides aminés, Trométhamine.
English descriptors
- KwdEn :
- Amino Acid Sequence, Circular Dichroism, Kinetics, Leucine (chemistry), Lysine (chemistry), Methanol (chemistry), Molecular Sequence Data, Oligopeptides (analysis), Oligopeptides (chemistry), Peptides (analysis), Peptides (chemistry), Protein Conformation, Protein Structure, Secondary, Solvents (chemistry), Spectrum Analysis, Spectrum Analysis, Raman, Tromethamine (chemistry).
- MESH :
- chemical , analysis : Oligopeptides, Peptides.
- chemical , chemistry : Leucine, Lysine, Methanol, Oligopeptides, Peptides, Solvents, Tromethamine.
- Amino Acid Sequence, Circular Dichroism, Kinetics, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Spectrum Analysis, Spectrum Analysis, Raman.
Abstract
Solution secondary structures of three synthetic cationic peptides, currently used in antisense oligonucleotide delivery into living cells, have been analyzed by means of circular dichroism (CD) and Raman scattering in different buffers as a function of concentration and time. All three peptides are of minimalist conception, i.e., formed by only two types of amino acids (leucine: L and lysine: K). Two of these peptides contain 15 aminoacids: N(ter)- KLLKLLLKLLLKLLK (L(10)K(5)), N(ter)-KLKLKLKLKLKLKLK (L(7)K(8)), and the third one has only 9 residues: N(ter)-KLKLKLKLK (L(4)K(5)). The conformational behavior of the 15-mers in pure water differs considerably one from another. Although both of them are initially disordered in the 50-350 microM range, L(10)K(5) gradually undergoes a disordered to alpha-helix transition for molecular concentrations above 100 microM. In all other solvents used, L(10)K(5) adopts a stable alpha-helical conformation. In methanol and methanol/Tris mixture, nonnative alpha-helices can be induced in both KL-alternating peptides, i.e., L(7)K(8) and L(4)K(5). However, in major cases and with a time delay depending on peptide concentration, beta-like structures can be gradually formed in both solutions. In PBS and methanol/PBS mixture, the tendency for L(7)K(8) and L(4)K(5) is to form structures belonging to beta-family. A discussion has been undertaken on the effect of counterions as well as their nature in the stabilization of ordered structures in both KL-alternating peptides.
DOI: 10.1002/bip.20366
PubMed: 16134172
Affiliations:
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pubmed:16134172Le document en format XML
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Coïc</name></author><author><name sortKey="Ghomi, Mahmoud" sort="Ghomi, Mahmoud" uniqKey="Ghomi M" first="Mahmoud" last="Ghomi">Mahmoud Ghomi</name></author></analytic><series><title level="j">Biopolymers</title><idno type="ISSN">0006-3525</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Kinetics</term><term>Leucine (chemistry)</term><term>Lysine (chemistry)</term><term>Methanol (chemistry)</term><term>Molecular Sequence Data</term><term>Oligopeptides (analysis)</term><term>Oligopeptides (chemistry)</term><term>Peptides (analysis)</term><term>Peptides (chemistry)</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Solvents (chemistry)</term><term>Spectrum Analysis</term><term>Spectrum Analysis, Raman</term><term>Tromethamine (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale</term><term>Analyse spectrale Raman</term><term>Cinétique</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Leucine ()</term><term>Lysine ()</term><term>Méthanol ()</term><term>Oligopeptides ()</term><term>Oligopeptides (analyse)</term><term>Peptides ()</term><term>Peptides (analyse)</term><term>Solvants ()</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Trométhamine ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Oligopeptides</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Leucine</term><term>Lysine</term><term>Methanol</term><term>Oligopeptides</term><term>Peptides</term><term>Solvents</term><term>Tromethamine</term></keywords><keywords 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secondary structures of three synthetic cationic peptides, currently used in antisense oligonucleotide delivery into living cells, have been analyzed by means of circular dichroism (CD) and Raman scattering in different buffers as a function of concentration and time. All three peptides are of minimalist conception, i.e., formed by only two types of amino acids (leucine: L and lysine: K). Two of these peptides contain 15 aminoacids: N(ter)- KLLKLLLKLLLKLLK (L(10)K(5)), N(ter)-KLKLKLKLKLKLKLK (L(7)K(8)), and the third one has only 9 residues: N(ter)-KLKLKLKLK (L(4)K(5)). The conformational behavior of the 15-mers in pure water differs considerably one from another. Although both of them are initially disordered in the 50-350 microM range, L(10)K(5) gradually undergoes a disordered to alpha-helix transition for molecular concentrations above 100 microM. In all other solvents used, L(10)K(5) adopts a stable alpha-helical conformation. In methanol and methanol/Tris mixture, nonnative alpha-helices can be induced in both KL-alternating peptides, i.e., L(7)K(8) and L(4)K(5). However, in major cases and with a time delay depending on peptide concentration, beta-like structures can be gradually formed in both solutions. In PBS and methanol/PBS mixture, the tendency for L(7)K(8) and L(4)K(5) is to form structures belonging to beta-family. A discussion has been undertaken on the effect of counterions as well as their nature in the stabilization of ordered structures in both KL-alternating peptides.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement><orgName><li>Université Pierre-et-Marie-Curie</li></orgName></list><tree><noCountry><name sortKey="Boukhalfa Heniche, F Z" sort="Boukhalfa Heniche, F Z" uniqKey="Boukhalfa Heniche F" first="F-Z" last="Boukhalfa-Heniche">F-Z Boukhalfa-Heniche</name><name sortKey="Coic, Yves Marie" sort="Coic, Yves Marie" uniqKey="Coic Y" first="Yves-Marie" last="Coïc">Yves-Marie Coïc</name><name sortKey="Ghomi, Mahmoud" sort="Ghomi, Mahmoud" uniqKey="Ghomi M" first="Mahmoud" last="Ghomi">Mahmoud Ghomi</name><name sortKey="Seksek, Olivier" sort="Seksek, Olivier" uniqKey="Seksek O" first="Olivier" last="Seksek">Olivier Seksek</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Hernandez, Belen" sort="Hernandez, Belen" uniqKey="Hernandez B" first="Belén" last="Hernández">Belén Hernández</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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