article · 01/10/2014
Low Concentration Structural Dynamics of Lanreotide and Somatostatin-14
Résumé
Lanreotide, a synthetic cyclic octapeptide, analogue of the peptide hormone somatostatin-14 (SST-14), is routinely used as a long-acting medication in the management of neuroendocrine tumors. Despite its therapeutic importance, low concentration structural data is still lacking for lanreotide. In fact, the major part of the previous structural investigations were focused on the remarkable aggregation properties of this peptide, appearing at high concentrations (> 5 mM). Here, we have applied three optical spectroscopic techniques, i. e. fluorescence, circular dichroism and Raman scattering, for analyzing the structural dynamics at the concentrations below 5 mM, where lanreotide exists either in a monomer state or at the first stages of aggregation. The obtained data from lanreotide were discussed through their comparison with those collected from SST-14, leading us to the following conclusions: (i) The central D-Trp residue, forming with its adjacent Lys the main receptor interacting part of lanreotide, keeps a constant high rotational freedom whatever the environment (water, water/methanol, methanol). (ii) A solvent-dependent tight beta-turn, belonging to the type-II' family, is revealed in lanreotide. (iii) Raman data analyzed by band decomposition in the amide (I and III) regions allowed estimation of different secondary structural elements within the millimolar range. Interestingly, the applied protocol shows a perfect agreement between the structural features provided by the amide I and amide III Raman markers. (C) 2014 Wiley Periodicals, Inc.
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Hernandez, B., Coic, Y.-M., Baron, B., Kruglik, S.-G., Pflueger, F., Cohen, R., Carelli, C., & Ghomi, M. (2014). Low Concentration Structural Dynamics of Lanreotide and Somatostatin-14. Biopolymers, 101(10), 1019-1028. https://doi.org/10.1002/bip.22491@article{Hernandez2014_23,
author = {Hernandez, Belen and Coic, Yves-Marie and Baron, Bruno and Kruglik, Sergei G. and Pflueger, Fernando and Cohen, Regis and Carelli, Claude and Ghomi, Mahmoud},
year = {2014},
month = {10},
title = {Low Concentration Structural Dynamics of Lanreotide and Somatostatin-14},
journal = {Biopolymers},
publisher = {WILEY-BLACKWELL},
volume = {101},
number = {10},
pages = {1019-1028},
address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
abstract = {Lanreotide, a synthetic cyclic octapeptide, analogue of the peptide hormone somatostatin-14 (SST-14), is routinely used as a long-acting medication in the management of neuroendocrine tumors. Despite its therapeutic importance, low concentration structural data is still lacking for lanreotide. In fact, the major part of the previous structural investigations were focused on the remarkable aggregation properties of this peptide, appearing at high concentrations (> 5 mM). Here, we have applied three optical spectroscopic techniques, i. e. fluorescence, circular dichroism and Raman scattering, for analyzing the structural dynamics at the concentrations below 5 mM, where lanreotide exists either in a monomer state or at the first stages of aggregation. The obtained data from lanreotide were discussed through their comparison with those collected from SST-14, leading us to the following conclusions: (i) The central D-Trp residue, forming with its adjacent Lys the main receptor interacting part of lanreotide, keeps a constant high rotational freedom whatever the environment (water, water/methanol, methanol). (ii) A solvent-dependent tight beta-turn, belonging to the type-II' family, is revealed in lanreotide. (iii) Raman data analyzed by band decomposition in the amide (I and III) regions allowed estimation of different secondary structural elements within the millimolar range. Interestingly, the applied protocol shows a perfect agreement between the structural features provided by the amide I and amide III Raman markers. (C) 2014 Wiley Periodicals, Inc.},
url = {http://www.dx.doi.org/10.1002/bip.22491},
doi = {10.1002/bip.22491},
issn = {0006-3525},
}TY - JOUR
AU - Hernandez, Belen
AU - Coic, Yves-Marie
AU - Baron, Bruno
AU - Kruglik, Sergei G.
AU - Pflueger, Fernando
AU - Cohen, Regis
AU - Carelli, Claude
AU - Ghomi, Mahmoud
PY - 2014
DA - 2014/10/01
TI - Low Concentration Structural Dynamics of Lanreotide and Somatostatin-14
JO - Biopolymers
VL - 101
IS - 10
PB - WILEY-BLACKWELL
SN - 0006-3525
AB - Lanreotide, a synthetic cyclic octapeptide, analogue of the peptide hormone somatostatin-14 (SST-14), is routinely used as a long-acting medication in the management of neuroendocrine tumors. Despite its therapeutic importance, low concentration structural data is still lacking for lanreotide. In fact, the major part of the previous structural investigations were focused on the remarkable aggregation properties of this peptide, appearing at high concentrations (> 5 mM). Here, we have applied three optical spectroscopic techniques, i. e. fluorescence, circular dichroism and Raman scattering, for analyzing the structural dynamics at the concentrations below 5 mM, where lanreotide exists either in a monomer state or at the first stages of aggregation. The obtained data from lanreotide were discussed through their comparison with those collected from SST-14, leading us to the following conclusions: (i) The central D-Trp residue, forming with its adjacent Lys the main receptor interacting part of lanreotide, keeps a constant high rotational freedom whatever the environment (water, water/methanol, methanol). (ii) A solvent-dependent tight beta-turn, belonging to the type-II' family, is revealed in lanreotide. (iii) Raman data analyzed by band decomposition in the amide (I and III) regions allowed estimation of different secondary structural elements within the millimolar range. Interestingly, the applied protocol shows a perfect agreement between the structural features provided by the amide I and amide III Raman markers. (C) 2014 Wiley Periodicals, Inc.
SP - 1019
EP - 1028
DO - 10.1002/bip.22491
UR - http://www.dx.doi.org/10.1002/bip.22491
ER -