Molecular features of steroid-binding antidins and their use for assaying serum progesterone

PloS One
Nitin AgrawalTomi T Airenne

Abstract

Chicken avidin (Avd) and streptavidin from Streptomyces avidinii are extensively used in bionanotechnology due to their extremely tight binding to biotin (Kd ~ 10-15 M for chicken Avd). We previously reported engineered Avds known as antidins, which have micro- to nanomolar affinities for steroids, non-natural ligands of Avd. Here, we report the 2.8 Å X-ray structure of the sbAvd-2 (I117Y) antidin co-crystallized with progesterone. We describe the creation of new synthetic phage display libraries and report the experimental as well as computational binding analysis of progesterone-binding antidins. We introduce a next-generation antidin with 5 nM binding affinity for progesterone, and demonstrate the use of antidins for measuring progesterone in serum samples. Our data give insights on how to engineer and alter the binding preferences of Avds and to develop better molecular tools for modern bionanotechnological applications.

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Citations

Jun 21, 2021·Nanomedicine : Nanotechnology, Biology, and Medicine·Ruchita ShandilyaPradyumna Kumar Mishra

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Methods Mentioned

BETA
phage display
X-ray
Differential scanning calorimetry
size
light scattering
PCA
ELISA
biolayer interferometry
dynamic light
static

Software Mentioned

MolProbity
OmniSEC
Refmac5
Discreet
Phaser
GraphPad Prism
Malign
Schrödinger
PRIME
GLIDE

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