File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Characterization of Surface-Active Biofilm Protein BslA in Self-Assembling Langmuir Monolayer at the Air-Water Interface

TitleCharacterization of Surface-Active Biofilm Protein BslA in Self-Assembling Langmuir Monolayer at the Air-Water Interface
Authors
Issue Date2017
Citation
Langmuir, 2017, v. 33, n. 30, p. 7548-7555 How to Cite?
Abstract© 2017 American Chemical Society. Biofilm is an extracellular matrix of bacteria and serves as a protective shield of bacterial communities. It is crucial for microbial growth and one of the leading causes of human chronic infections as well. However, the structures and molecular mechanism of biofilm formation remain largely unknown. Here, we examined a protein, BslA, expressed in the biofilms of Bacillus subtilis. We characterized the Langmuir monolayers of BslA at the air/water interface. Using techniques in surface chemistry and spectroscopy, we found that BslA forms a stable and robust Langmuir monolayer at the air/water interface. Our results show that the BslA Langmuir monolayer underwent two-stage elasticity in the solid state phase upon mechanical compression: one is possibly due to the intermolecular interaction and the other is likely due to both the intermolecular compulsion and the intramolecular distortion. The Langmuir monolayer of BslA shows abrupt changes in rigidities and elasticities at ∼25 mN/m. This surface pressure is close to the one at which BlsA saturates the air/water interface as a self-assembled film without mechanical compression, corresponding to a mean molecular area of ∼700 Å2 per molecule. Based on the results of surface UV-visible spectroscopy and infrared reflective-absorption spectroscopy, we propose that the BslA Langmuir monolayer carries intermolecular elasticity before ∼25 mN/m and both intermolecular and intramolecular elasticity after ∼25 mN/m. These results provide valuable insights into the understanding of biofilm-associated protein under high mechanical force, shedding light on further investigation of biofilm structure and functionalities.
Persistent Identifierhttp://hdl.handle.net/10722/283651
ISSN
2023 Impact Factor: 3.7
2023 SCImago Journal Rankings: 0.786
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Wei-
dc.contributor.authorLi, Shanghao-
dc.contributor.authorWang, Zhuguang-
dc.contributor.authorYan, Elsa C.Y.-
dc.contributor.authorLeblanc, Roger M.-
dc.date.accessioned2020-07-03T08:07:53Z-
dc.date.available2020-07-03T08:07:53Z-
dc.date.issued2017-
dc.identifier.citationLangmuir, 2017, v. 33, n. 30, p. 7548-7555-
dc.identifier.issn0743-7463-
dc.identifier.urihttp://hdl.handle.net/10722/283651-
dc.description.abstract© 2017 American Chemical Society. Biofilm is an extracellular matrix of bacteria and serves as a protective shield of bacterial communities. It is crucial for microbial growth and one of the leading causes of human chronic infections as well. However, the structures and molecular mechanism of biofilm formation remain largely unknown. Here, we examined a protein, BslA, expressed in the biofilms of Bacillus subtilis. We characterized the Langmuir monolayers of BslA at the air/water interface. Using techniques in surface chemistry and spectroscopy, we found that BslA forms a stable and robust Langmuir monolayer at the air/water interface. Our results show that the BslA Langmuir monolayer underwent two-stage elasticity in the solid state phase upon mechanical compression: one is possibly due to the intermolecular interaction and the other is likely due to both the intermolecular compulsion and the intramolecular distortion. The Langmuir monolayer of BslA shows abrupt changes in rigidities and elasticities at ∼25 mN/m. This surface pressure is close to the one at which BlsA saturates the air/water interface as a self-assembled film without mechanical compression, corresponding to a mean molecular area of ∼700 Å2 per molecule. Based on the results of surface UV-visible spectroscopy and infrared reflective-absorption spectroscopy, we propose that the BslA Langmuir monolayer carries intermolecular elasticity before ∼25 mN/m and both intermolecular and intramolecular elasticity after ∼25 mN/m. These results provide valuable insights into the understanding of biofilm-associated protein under high mechanical force, shedding light on further investigation of biofilm structure and functionalities.-
dc.languageeng-
dc.relation.ispartofLangmuir-
dc.titleCharacterization of Surface-Active Biofilm Protein BslA in Self-Assembling Langmuir Monolayer at the Air-Water Interface-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/acs.langmuir.7b01739-
dc.identifier.pmid28701036-
dc.identifier.scopuseid_2-s2.0-85026769840-
dc.identifier.volume33-
dc.identifier.issue30-
dc.identifier.spage7548-
dc.identifier.epage7555-
dc.identifier.eissn1520-5827-
dc.identifier.isiWOS:000406982400020-
dc.identifier.issnl0743-7463-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats