Unknown

Dataset Information

0

Labeled protein recognition at a membrane bilayer interface by embedded synthetic receptors.


ABSTRACT: Self-folding deep cavitands embedded in a supported lipid bilayer are capable of recognizing suitably labeled proteins at the bilayer interface. The addition of a choline derived binding "handle" to a number of different proteins allows their selective noncovalent recognition, with association constants on the order of 10(5) M(-1). The proteins are displayed at the water:bilayer interface, and a single binding handle allows recognition of the large, charged protein by a small molecule synthetic receptor via complementary shape and charge interactions.

SUBMITTER: Ghang YJ 

PROVIDER: S-EPMC4176395 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Labeled protein recognition at a membrane bilayer interface by embedded synthetic receptors.

Ghang Yoo-Jin YJ   Lloyd Jonathan J JJ   Moehlig Melissa P MP   Arguelles Jessica K JK   Mettry Magi M   Zhang Xing X   Julian Ryan R RR   Cheng Quan Q   Hooley Richard J RJ  

Langmuir : the ACS journal of surfaces and colloids 20140819 34


Self-folding deep cavitands embedded in a supported lipid bilayer are capable of recognizing suitably labeled proteins at the bilayer interface. The addition of a choline derived binding "handle" to a number of different proteins allows their selective noncovalent recognition, with association constants on the order of 10(5) M(-1). The proteins are displayed at the water:bilayer interface, and a single binding handle allows recognition of the large, charged protein by a small molecule synthetic  ...[more]

Similar Datasets

| S-EPMC5062009 | biostudies-literature
| S-EPMC4706080 | biostudies-literature
| S-EPMC5857991 | biostudies-literature
| S-EPMC8015139 | biostudies-literature
| S-EPMC6452872 | biostudies-literature
| S-EPMC5537337 | biostudies-literature
| S-EPMC8179348 | biostudies-literature
| S-EPMC5364453 | biostudies-literature
| S-EPMC8671107 | biostudies-literature
| S-EPMC8634737 | biostudies-literature