Evidence map›Paper›PMID 33928264›Full record

ArticleCell reports. Physical science2021

Solid-state packing dictates the unexpected solubility of aromatic peptides.

Santu Bera, Xuewei Dong, Bankala Krishnarjuna, Shannon A Raab, David A Hales, Wei Ji, Yiming Tang, Linda J W Shimon, Ayyalusamy Ramamoorthy, David E Clemmer and 2 more

Abstract read
In one paragraph

Article in Cell reports. Physical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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

12 authors.

Santu BeraShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel.
Xuewei DongDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Bankala KrishnarjunaBiophysics Program, Department of Chemistry, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA.
Shannon A RaabDepartment of Chemistry, Indiana University, 800 Kirkwood Avenue, Bloomington, IN 47401, USA.
David A HalesDepartment of Chemistry, Indiana University, 800 Kirkwood Avenue, Bloomington, IN 47401, USA.
Wei JiShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel.
Yiming TangDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Linda J W ShimonDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ayyalusamy RamamoorthyBiophysics Program, Department of Chemistry, Macromolecular Science and Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA.
David E ClemmerDepartment of Chemistry, Indiana University, 800 Kirkwood Avenue, Bloomington, IN 47401, USA.
Guanghong WeiDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (MOE), Fudan University, Shanghai, 200433, People's Republic of China.
Ehud GazitShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel.

Funding

Development of high resolution mobility measurements for structural biologyR01GM121751 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., LAGANOWSKY, ARTHUR D · 2017 to 2020
$1.7M
NIGMS NIH HHS R01 GM121751
6 · The paper itself

Abstract

The understanding and prediction of the solubility of biomolecules, even of the simplest ones, reflect an open question and unmet need. Short aromatic tripeptides are among the most highly aggregative biomolecules. However, in marked contrast, Ala-Phe-Ala (AFA) was surprisingly found to be non-aggregative and could be solubilized at millimolar concentrations. Here, aiming to uncover the underlying molecular basis of its high solubility, we explore in detail the solubility, aggregation propensity, and atomic-level structure of the tripeptide. We demonstrate an unexpectedly high water solubility of AFA reaching 672 mM, two orders of magnitude higher than reported previously. The single crystal structure reveals an anti-parallel β sheet conformation devoid of any aromatic interactions. This study provides clear mechanistic insight into the structural basis of solubility and suggests a simple and feasible tool for its estimation, bearing implications for design of peptide drugs, peptides materials, and advancement of peptide nanotechnology.

Indexed as

aggregationAromatic peptidecrystal packing-solubility relationshipmass spectrometryNMR spectroscopy

Identifiers

PMID33928264
PMCPMC8063180

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

None linked

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.