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Angel Luis Pey on Muck Rack

Angel Luis Pey

As seen in: BioRxiv
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Articles

The lack of trade-off between conformational stability and binding affinity in a nanobody with therapeutic potential for a misfolding disease

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By Atanasio Gómez-Mulas, Athi N. Naganathan, Angel Luis Pey, Facultad de Ciencias
| BioRxiv
Abstract To improve protein pharmaceuticals, we need to balance protein stability and binding affinity with in vivo efficiency. We have recently developed a nanobody (NB-AGT-2) against the alanine:glyoxylate aminotransferase with high stability (Tm~85°C) that may be useful to treat a misfolding disease called primary hyperoxaluria type 1.
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Thermodynamic versus kinetic basis for the high conformational stability of nanobodies for therapeutic applications

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By Atanasio Gómez-Mulas, Eduardo Salido, Angel Luis Pey, Universidad de Granada
| BioRxiv
Abstract Single domain nanobodies (NB) are powerful tools for biotechnological and therapeutic applications. They strongly bind to their targets and are very stable. Early studies showed that NB unfolding is reversible and can be analyzed by equilibrium thermodynamics whereas more recent studies focused on their kinetic stability in very harsh conditions, far from storage or physiological temperatures (4-37oC).
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Structural dynamics and functional cooperativity of human NQO1 by ambient temperature serial crystallography and simulations

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By Alice Grieco, José Gavira Verified, Sergio Boneta, Angel Luis Pey
| BioRxiv
Abstract The human NQO1 (hNQO1) is a FAD-dependent oxidoreductase that catalyzes the two-electron reduction of quinones to hydroquinones, being essential for the antioxidant defense system, stabilization of tumor suppressors, and activation of quinone-based chemotherapeutics, and it is over-expressed in several tumors, which makes it an attractive cancer drug target.
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