TY - JOUR
T1 - Modulation of the Interaction between a Peptide Ligand and a G Protein-Coupled Receptor by Halogen Atoms
AU - Rosa, Mònica
AU - Caltabiano, Gianluigi
AU - Barreto-Valer, Katy
AU - Gonzalez-Nunez, Verónica
AU - Gómez-Tamayo, José C.
AU - Ardá, Ana
AU - Jiménez-Barbero, Jesús
AU - Pardo, Leonardo
AU - Rodríguez, Raquel E.
AU - Arsequell, Gemma
AU - Valencia, Gregorio
PY - 2015/8/13
Y1 - 2015/8/13
N2 - © 2015 American Chemical Society. Systematic halogenation of two native opioid peptides has shown that halogen atoms can modulate peptide-receptor interactions in different manners. First, halogens may produce a steric hindrance that reduces the binding of the peptide to the receptor. Second, chlorine, bromine, or iodine may improve peptide binding if their positive σ-hole forms a halogen bond interaction with negatively charged atoms of the protein. Lastly, the negative electrostatic potential of fluorine can interact with positively charged atoms of the protein to improve peptide binding.
AB - © 2015 American Chemical Society. Systematic halogenation of two native opioid peptides has shown that halogen atoms can modulate peptide-receptor interactions in different manners. First, halogens may produce a steric hindrance that reduces the binding of the peptide to the receptor. Second, chlorine, bromine, or iodine may improve peptide binding if their positive σ-hole forms a halogen bond interaction with negatively charged atoms of the protein. Lastly, the negative electrostatic potential of fluorine can interact with positively charged atoms of the protein to improve peptide binding.
KW - drug design
KW - endomorphin-1
KW - G protein-coupled receptors
KW - Halogen bond
KW - halogenated peptides
KW - Leu-enkephalin
KW - neuropeptides
KW - opioid receptors
U2 - 10.1021/acsmedchemlett.5b00126
DO - 10.1021/acsmedchemlett.5b00126
M3 - Article
SN - 1948-5875
VL - 6
SP - 872
EP - 876
JO - ACS Medicinal Chemistry Letters
JF - ACS Medicinal Chemistry Letters
IS - 8
ER -