TY - JOUR
T1 - Proton- versus Cation-Selective Transport of Saccharide Rim-Appended Pillar[5]arene Artificial Water Channels
AU - Andrei, Iuliana M.
AU - Chen, Wenzhang
AU - Baaden, Marc
AU - Vincent, Stéphane P.
AU - Barboiu, Mihail
N1 - Publisher Copyright:
© 2023 American Chemical Society.
PY - 2023/10/11
Y1 - 2023/10/11
N2 - Transport of water across cell membranes is a fundamental process for important biological functions. Herein, we focused our research on a new type of symmetrical saccharide rim-functionalized pillar[5]arene (PA-S) artificial water channels with variable pore structures. To point out the versatility of PA-S channels, we systematically varied the nature of anchoring/gate keepers d-mannoside, d-mannuronic acid, or sialic acid H-bonding groups on lateral pillar[5]arene (PA) arms, known as good membrane adhesives, to best describe the influence of the chemical structure on their transport activity. The control of hydrophobic membrane binding-hydrophilic water binding balance is an important feature influencing the channels’ structuration and efficiency for a proper insertion into bilayer membranes. The glycosylated PA channels’ transport performances were assessed in lipid bilayer membranes, and the channels were able to transport water at high rates (∼106-107 waters/s/channel within 1 order of magnitude as for aquaporins), serving as selective proton railways with total Na+ and K+ rejection. Molecular simulation substantiates the idea that the PAs can generate supramolecular pores, featuring hydrophilic carbohydrate gate-keepers that serve as water-sponge relays at the channel entrance, effectively absorbing and redirecting water within the channel. The present channels may be regarded as a rare biomimetic example of artificial channels presenting proton vs cation transport selectivity performances.
AB - Transport of water across cell membranes is a fundamental process for important biological functions. Herein, we focused our research on a new type of symmetrical saccharide rim-functionalized pillar[5]arene (PA-S) artificial water channels with variable pore structures. To point out the versatility of PA-S channels, we systematically varied the nature of anchoring/gate keepers d-mannoside, d-mannuronic acid, or sialic acid H-bonding groups on lateral pillar[5]arene (PA) arms, known as good membrane adhesives, to best describe the influence of the chemical structure on their transport activity. The control of hydrophobic membrane binding-hydrophilic water binding balance is an important feature influencing the channels’ structuration and efficiency for a proper insertion into bilayer membranes. The glycosylated PA channels’ transport performances were assessed in lipid bilayer membranes, and the channels were able to transport water at high rates (∼106-107 waters/s/channel within 1 order of magnitude as for aquaporins), serving as selective proton railways with total Na+ and K+ rejection. Molecular simulation substantiates the idea that the PAs can generate supramolecular pores, featuring hydrophilic carbohydrate gate-keepers that serve as water-sponge relays at the channel entrance, effectively absorbing and redirecting water within the channel. The present channels may be regarded as a rare biomimetic example of artificial channels presenting proton vs cation transport selectivity performances.
UR - http://www.scopus.com/inward/record.url?scp=85173583094&partnerID=8YFLogxK
U2 - 10.1021/jacs.3c06335
DO - 10.1021/jacs.3c06335
M3 - Article
C2 - 37771004
AN - SCOPUS:85173583094
SN - 0002-7863
VL - 145
SP - 21904
EP - 21914
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 40
ER -