Surface-Induced Hydrophobin Assemblies with Versatile Properties and Distinct Underlying Structures.

Fungal Proteins / chemistry Wettability Hydrophobic and Hydrophilic Interactions Surface Properties Amino Acid Sequence Amyloid / chemistry Amyloidogenic Proteins

Journal

Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849

Informations de publication

Date de publication:
13 11 2023
Historique:
medline: 14 11 2023
pubmed: 25 9 2023
entrez: 25 9 2023
Statut: ppublish

Résumé

Hydrophobins are remarkable proteins due to their ability to self-assemble into amphipathic coatings that reverse surface wettability. Here, the versatility of the Class I hydrophobins EAS

Identifiants

DOI: 10.1021/acs.biomac.3c00542 PMID: 37747808
pubmed: 37747808
doi: 10.1021/acs.biomac.3c00542
doi:

Substances chimiques

Fungal Proteins 0
Amyloid 0
Amyloidogenic Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4783-4797

Auteurs

Rezwan Siddiquee (R)

School of Life and Environmental Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.

Victor Lo (V)

School of Medical Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.

Caitlin L Johnston (CL)

School of Medical Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.

Aston W Buffier (AW)

School of Life and Environmental Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.

Sarah R Ball (SR)

Formerly at School of Medical Sciences, The University of Sydney, Sydney, NSW 2006, Australia.

Jonathan L Ciofani (JL)

School of Medicine, The University of Sydney, Sydney, NSW 2006, Australia.

Yi Cheng Zeng (YC)

Formerly at School of Life and Environmental Sciences, The University of Sydney, Sydney, NSW 2006, Australia.

Mahiar Mahjoub (M)

School of Medicine, The University of Sydney, Sydney, NSW 2006, Australia.

Wojciech Chrzanowski (W)

Sydney Pharmacy School, The University of Sydney, Sydney, NSW 2006, Australia.

Shahrzad Rezvani-Baboli (S)

School of Natural Sciences, Macquarie University, Sydney, NSW 2109, Australia.
ORCID: 0000-0002-0132-4213

Louise Brown (L)

School of Natural Sciences, Macquarie University, Sydney, NSW 2109, Australia.

Chi L L Pham (CLL)

Formerly at School of Medical Sciences, The University of Sydney, Sydney, NSW 2006, Australia.

Margaret Sunde (M)

School of Medical Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.
ORCID: 0000-0002-0150-3203

Ann H Kwan (AH)

School of Life and Environmental Sciences and Sydney Nano, The University of Sydney, Sydney, NSW 2006, Australia.
ORCID: 0000-0002-1506-2226

Articles similaires

Decoding the genomic terrain: functional insights into 14 chemosensory proteins in whitefly Bemisia tabaci Asia II-1.

M N Rudra Gouda, Sabtharishi Subramanian
1.00
Animals Hemiptera Insect Proteins Phylogeny Insecticides

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.

Arpine Sokratian, Ye Zhou, Meltem Tatli et al.
1.00
alpha-Synuclein Humans Animals Mice Lewy Body Disease

Menthol as an effective inhibitor of quorum sensing and biofilm formation in Candida albicans and Candida glabrata by targeting the transcriptional repressor TUP1.

Pouria Khodavandi, Maryam Miri Soogh, Fahimeh Alizadeh et al.
1.00
Biofilms Candida albicans Quorum Sensing Candida glabrata Menthol

Motif mapping during chickpea germination reveals a complex sequential activation of different proteolytic activities.

Indrani Bera, Michael O'Sullivan, Caitriona Scaife et al.
1.00
Cicer Germination Proteolysis Seeds Plant Proteins

Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Phénomènes chimiques › Propriétés de surface › Mouillabilité › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Phénomènes chimiques › Interactions hydrophobes et hydrophiles › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Phénomènes chimiques › Propriétés de surface › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Sciences de l'information › Sources d'information › Services d'information › Documentation › Données de séquences moléculaires › Séquence d'acides aminés › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Amyloïde › Surface-Induced Hydrophobin Assemblies with...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Amyloïde › Protéines amyloïdogènes › Surface-Induced Hydrophobin Assemblies with...