TY - JOUR
T1 - Supramolecular chemistry targeting proteins
AU - van Dun, S.
AU - Ottmann, C.
AU - Milroy, L.-G.
AU - Brunsveld, L.
PY - 2017/10/11
Y1 - 2017/10/11
N2 - The specific recognition of protein surface elements is a fundamental challenge in the life sciences. New developments in this field will form the basis of advanced therapeutic approaches and lead to applications such as sensors, affinity tags, immobilization techniques, and protein-based materials. Synthetic supramolecular molecules and materials are creating new opportunities for protein recognition that are orthogonal to classical small molecule and protein-based approaches. As outlined here, their unique molecular features enable the recognition of amino acids, peptides, and even whole protein surfaces, which can be applied to the modulation and assembly of proteins. We believe that structural insights into these processes are of great value for the further development of this field and have therefore focused this Perspective on contributions that provide such structural data.
AB - The specific recognition of protein surface elements is a fundamental challenge in the life sciences. New developments in this field will form the basis of advanced therapeutic approaches and lead to applications such as sensors, affinity tags, immobilization techniques, and protein-based materials. Synthetic supramolecular molecules and materials are creating new opportunities for protein recognition that are orthogonal to classical small molecule and protein-based approaches. As outlined here, their unique molecular features enable the recognition of amino acids, peptides, and even whole protein surfaces, which can be applied to the modulation and assembly of proteins. We believe that structural insights into these processes are of great value for the further development of this field and have therefore focused this Perspective on contributions that provide such structural data.
KW - Journal Article
UR - http://www.scopus.com/inward/record.url?scp=85031102095&partnerID=8YFLogxK
U2 - 10.1021/jacs.7b01979
DO - 10.1021/jacs.7b01979
M3 - Article
C2 - 28926241
VL - 139
SP - 13960
EP - 13968
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 40
ER -