Evidence map›Paper›PMID 32624891›Full record

ReviewEngineering in life sciences2018

Experimental characterization and simulation of amino acid and peptide interactions with inorganic materials.

Sebastian Schwaminger, Silvia Angela Blank-Shim, Monika Borkowska-Panek, Priya Anand, Paula Fraga-García, Karin Fink, Wolfgang Wenzel, Sonja Berensmeier

Open access · bronzeAbstract readReview
In one paragraph

Review in Engineering in life sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
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

6 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Buffer Influence on the Amino Acid Silica Interaction.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020
    Article
  5. Article
  6. Article
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

8 authors at 2 institutions in 1 country.

Sebastian SchwamingerBioseparation Engineering Group Technical University of Munich München Germany.ORCID 0000-0002-8627-0807
Silvia Angela Blank-ShimBioseparation Engineering Group Technical University of Munich München Germany.ORCID 0000-0003-0239-8545
Monika Borkowska-PanekInstitute of Nanotechnology Karlsruhe Institute of Technology Karlsruhe Germany.
Priya AnandInstitute of Nanotechnology Karlsruhe Institute of Technology Karlsruhe Germany.
Paula Fraga-GarcíaBioseparation Engineering Group Technical University of Munich München Germany.
Karin FinkInstitute of Nanotechnology Karlsruhe Institute of Technology Karlsruhe Germany.
Wolfgang WenzelInstitute of Nanotechnology Karlsruhe Institute of Technology Karlsruhe Germany.
Sonja BerensmeierBioseparation Engineering Group Technical University of Munich München Germany.ORCID 0000-0002-4943-848X
Karlsruhe Institute of Technology · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inspired by nature, many applications and new materials benefit from the interplay of inorganic materials and biomolecules. A fundamental understanding of complex organic-inorganic interactions would improve the controlled production of nanomaterials and biosensors to the development of biocompatible implants for the human body. Although widely exploited in applications, the interaction of amino acids and peptides with most inorganic surfaces is not fully understood. To date, precisely characterizing complex surfaces of inorganic materials and analyzing surface-biomolecule interactions remain challenging both experimentally and computationally. This article reviews several approaches to characterizing biomolecule-surface interactions and illustrates the advantages and disadvantages of the methods presented. First, we explain how the adsorption mechanism of amino acids/peptides to inorganic surfaces can be determined and how thermodynamic and kinetic process constants can be obtained. Second, we demonstrate how this data can be used to develop models for peptide-surface interactions. The understanding and simulation of such interactions constitute a basis for developing molecules with high affinity binding domains in proteins for bioprocess engineering and future biomedical technologies.

Indexed as

AdsorptionAmino acidInorganic surfaceInteractionPeptide

Identifiers

PMID32624891
PMCPMC6999452
OpenAlexW2729148804

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.