TY - JOUR
T1 - Identification of hot regions of the Aβ-IAPP Interaction interface as high-affinity binding sites in both cross- and self-association
AU - Andreetto, Erika
AU - Yan, Li Mei
AU - Tatarek-Nossol, Marianna
AU - Velkova, Aleksandra
AU - Frank, Ronald
AU - Kapurniotu, Aphrodite
PY - 2010/4/12
Y1 - 2010/4/12
N2 - (Figure Presented) Short peptide sequences are identified as hot regions of the cross-interaction interface of the Alzheimer's disease β-amyloid peptide (Aβ) with the type 2 diabetes islet amyloid polypeptide (IAPP). They are shown to be high-affinity ligands of both Aβ and IAPP, thus suggesting common molecular recognition features in amyloid self- and cross-amyloid hetero-assembly.
AB - (Figure Presented) Short peptide sequences are identified as hot regions of the cross-interaction interface of the Alzheimer's disease β-amyloid peptide (Aβ) with the type 2 diabetes islet amyloid polypeptide (IAPP). They are shown to be high-affinity ligands of both Aβ and IAPP, thus suggesting common molecular recognition features in amyloid self- and cross-amyloid hetero-assembly.
KW - Islet amyloid polypeptides
KW - Molecular recognition
KW - Protein interactions
KW - Protein self-assembly
KW - β-amyloid peptides
UR - http://www.scopus.com/inward/record.url?scp=77951177586&partnerID=8YFLogxK
U2 - 10.1002/anie.200904902
DO - 10.1002/anie.200904902
M3 - Article
C2 - 20309983
AN - SCOPUS:77951177586
SN - 1433-7851
VL - 49
SP - 3081
EP - 3085
JO - Angewandte Chemie International Edition in English
JF - Angewandte Chemie International Edition in English
IS - 17
ER -
