Conformational analysis of neuropeptide Y-[18–36] analogs in hydrophobic environments
The interactive and conformational behavior of a series of neuropeptide Y-[18–36] (NPY-[18–36]) analogs in hydrophobic environments have been investigated using reversed-phase high-performance liquid chromatography (RP-HPLC) and circular dichroism (CD) spectroscopy. The peptides studied comprised a...
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Published in | Biophysical journal Vol. 72; no. 1; pp. 238 - 246 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
1997
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Abstract | The interactive and conformational behavior of a series of neuropeptide Y-[18–36] (NPY-[18–36]) analogs in hydrophobic environments have been investigated using reversed-phase high-performance liquid chromatography (RP-HPLC) and circular dichroism (CD) spectroscopy. The peptides studied comprised a series of 16 analogs of NPY-[18–36], each containing a single D-amino acid substitution. The influence of these single L-->D substitutions on the alpha-helical conformation of the NPY-[18–36] analogs in different solvent environments was determined by CD spectroscopy. Retention parameters related to the hydrophobic contact area and the affinity of interaction were determined with an n-octadecyl (C18) adsorbent. Structural transitions for all peptides were manifested as significant changes in the hydrophobic binding domain and surface affinity between 4 degrees C and 37 degrees C. The results indicated that the central region of NPY-[18–36] (residues 23–33) is important for maintenance of the alpha-helical conformation. Moreover, L-->D amino acid residue substitutions within the N- and C-terminal regions, as well as Asn29 and Leu30, do not appear to affect the secondary structure of the peptide. These studies demonstrate that RP-HPLC provides a powerful adjunct for investigations into the induction of stabilized secondary structure in peptides upon their interaction with hydrophobic surfaces. |
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AbstractList | The interactive and conformational behavior of a series of neuropeptide Y-[18–36] (NPY-[18–36]) analogs in hydrophobic environments have been investigated using reversed-phase high-performance liquid chromatography (RP-HPLC) and circular dichroism (CD) spectroscopy. The peptides studied comprised a series of 16 analogs of NPY-[18–36], each containing a single D-amino acid substitution. The influence of these single L-->D substitutions on the alpha-helical conformation of the NPY-[18–36] analogs in different solvent environments was determined by CD spectroscopy. Retention parameters related to the hydrophobic contact area and the affinity of interaction were determined with an n-octadecyl (C18) adsorbent. Structural transitions for all peptides were manifested as significant changes in the hydrophobic binding domain and surface affinity between 4 degrees C and 37 degrees C. The results indicated that the central region of NPY-[18–36] (residues 23–33) is important for maintenance of the alpha-helical conformation. Moreover, L-->D amino acid residue substitutions within the N- and C-terminal regions, as well as Asn29 and Leu30, do not appear to affect the secondary structure of the peptide. These studies demonstrate that RP-HPLC provides a powerful adjunct for investigations into the induction of stabilized secondary structure in peptides upon their interaction with hydrophobic surfaces. The interactive and conformational behavior of a series of neuropeptide Y-[18-36] (NPY-[18-36]) analogs in hydrophobic environments have been investigated using reversed-phase high-performance liquid chromatography (RP-HPLC) and circular dichroism (CD) spectroscopy. The peptides studied comprised a series of 16 analogs of NPY-[18-36], each containing a single D-amino acid substitution. The influence of these single L-->D substitutions on the alpha-helical conformation of the NPY-[18-36] analogs in different solvent environments was determined by CD spectroscopy. Retention parameters related to the hydrophobic contact area and the affinity of interaction were determined with an n-octadecyl (C18) adsorbent. Structural transitions for all peptides were manifested as significant changes in the hydrophobic binding domain and surface affinity between 4 degrees C and 37 degrees C. The results indicated that the central region of NPY-[18-36] (residues 23-33) is important for maintenance of the alpha-helical conformation. Moreover, L-->D amino acid residue substitutions within the N- and C-terminal regions, as well as Asn29 and Leu30, do not appear to affect the secondary structure of the peptide. These studies demonstrate that RP-HPLC provides a powerful adjunct for investigations into the induction of stabilized secondary structure in peptides upon their interaction with hydrophobic surfaces. |
Author | Bayer, E. Lazoura, E. Aguilar, M.I. Maidonis, I. Hearn, M.T. |
AuthorAffiliation | Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8994608$$D View this record in MEDLINE/PubMed |
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SubjectTerms | Amino Acid Sequence Angiotensin I - chemistry Angiotensin II - chemistry Angiotensin III - chemistry Chromatography, High Pressure Liquid Circular Dichroism Models, Structural Molecular Sequence Data Neuropeptide Y - chemistry Peptide Fragments - chemistry Peptides - chemistry Protein Conformation Protein Structure, Secondary Structure-Activity Relationship Thermodynamics |
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Title | Conformational analysis of neuropeptide Y-[18–36] analogs in hydrophobic environments |
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