Evidence map›Paper›PMID 39593207›Full record

ArticleFEBS letters2025

Thermodynamic versus kinetic basis for the high conformational stability of nanobodies for therapeutic applications.

Atanasio Gómez-Mulas, Mario Cano-Muñoz, Eduardo Salido Ruiz, Angel Luis Pey

Abstract read
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Atanasio Gómez-MulasDepartamento de Química Física, Universidad de Granada, Spain.
Mario Cano-MuñozDepartamento de Química Física, Universidad de Granada, Spain.
Eduardo Salido RuizCenter for Rare Diseases (CIBERER), Hospital Universitario de Canarias, Universidad de la Laguna, Tenerife, Spain.
Angel Luis PeyDepartamento de Química Física, Unidad de Excelencia en Química Aplicada a Biomedicina y Medioambiente e Instituto de Biotecnología, Universidad de Granada, Spain.ORCID 0000-0001-7706-3243

Funding

Consejería de Economía, Conocimiento, Empresas y Universidad, Junta de Andalucía P18-RT-2413Postdoctoral Research Program, Juan de la Cierva JDC2022-049681-IUniversidad de Granada
6 · The paper itself

Abstract

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 that are far from storage or physiological temperatures (4-37 °C). Here, we show that the thermodynamic view of NB stability holds in a wide range of temperatures (18-100 °C). The thermodynamic stability of three different NBs did not correlate with binding affinity for their target. Alpha-Fold 2 analyses of these NBs showed structural differences in the binding site and hydrogen bond networks. We expect that our approach will be helpful to improve our capacity to enhance structure-function-stability relationships of NB.

Indexed as

Single-Domain AntibodiesHumansHydrogen BondingKineticsProtein ConformationProtein StabilityTemperatureThermodynamicsSingle-Domain Antibodiesconformational stabilitynanobodiesprotein unfoldingtherapeuticsthermodynamics

Identifiers

PMID39593207
PMCPMC11891404

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.