Effect of concentration and denaturation on adsorption and surface tension of bovine serum albumin

McClellan, Scott J; Franses, Elias I.

doi:10.1016/s0927-7765(02)00131-5

Cited by 133 publications

(134 citation statements)

References 26 publications

Supporting

Mentioning

118

Contrasting

Order By: Relevance

“…After BSA adsorption, the surface nm. 45 The pitch of the profile after BSA adsorption matches that of the original copolymer surface. (26) copolymer, which presents a striped pattern (Figure 4a and 4b).…”

Section: Bsa Adsorption On the Copolymer Templatesmentioning

confidence: 81%

Protein Nanopatterning on Self-Organized Poly(styrene-b-isoprene) Thin Film Templates

2009

View full text Add to dashboard Cite

Abstract:Templated surfaces can be used to create patterns of proteins for applications in cell biology, bio-sensors and tissue engineering. A diblock copolymer template, which contains a pair of hydrophobic blocks, has been developed. The template is created from well-ordered, non-equilibrium surface structures of poly(styrene-b-isoprene) (PS-b-PI) diblock copolymers, which are achieved in ultrathin films having a thickness less than one domain period. Adsorption and nanopatterning of bovine serum albumin (BSA) on these thin films were studied. After incubation of the copolymer templates in BSA solutions (500 µg/ml) for a period of one hour, BSA molecules formed either a striped or a dense, ring-like structure, closely resembling the underlying polymer templates. In this "hard-soft" PS-b-PI system, BSA molecules were preferentially adsorbed on the hard PS domains, rather than on the soft PI domains. SIMS and contact angle analysis revealed that with more PI localized at the free surface, fewer BSA molecules were adsorbed. SIMS analysis confirmed that BSA molecules were adsorbed selectively on the PS blocks. This is the first example of two hydrophobic blocks of a diblock copolymer being used as a protein patterning template. Previously reported diblock copolymer templates used hydrophilic and hydrophobic pairs. A potentially useful characteristic of this template is that it is effective at high protein solution concentrations (up to 1 mg/ml) and for long incubation times (up to two hours), which broadens its range of applicability in various uses.

show abstract

Section: Bsa Adsorption On the Copolymer Templatesmentioning

confidence: 81%

Protein Nanopatterning on Self-Organized Poly(styrene-b-isoprene) Thin Film Templates

2009

View full text Add to dashboard Cite

show abstract

“…More recently also external reflection circular dichroism has been used to assess this information [33]. From a combination of these techniques, several authors conclude that only limited changes in the conformation of proteins occurs upon adsorption at the air-water interface [28,32,34,[36][37][38][39][40]. Maximum changes of up to 10% are observed in the secondary structure, but the globular folding state of the protein is generally found to remain intact [34].…”

Section: Introductionmentioning

confidence: 99%

The adsorption and unfolding kinetics determines the folding state of proteins at the air–water interface and thereby the equation of state

Wierenga¹,

Egmond²,

Voragen³

et al. 2006

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

Unfolding of proteins has often been mentioned as an important factor during the adsorption process at air-water interfaces and in the increase of surface pressure at later stages of the adsorption process. This work focuses on the question whether the folding state of the adsorbed protein depends on the rate of adsorption to the interface, which can be controlled by bulk concentration. Therefore, the adsorption of proteins with varying structural stabilities at several protein concentrations was studied using ellipsometry and surface tensiometry. For β-lactoglobulin the adsorbed amount (Γ ) needed to reach a certain surface pressure (Π) decreased with decreasing bulk concentration. Ovalbumin showed no such dependence. To verify whether this difference in behavior is caused by the difference in structural stability, similar experiments were performed with cytochrome c and a destabilized variant of this protein. Both proteins showed identical Π-Γ , and no dependence on bulk concentration. From this work it was concluded that unfolding will only take place if the kinetics of adsorption is similar or slower than the kinetics of unfolding. The latter depends on the activation energy of unfolding (which is in the order of 100-300 kJ/mol), rather than the free energy of unfolding (typically 10-50 kJ/mol).

show abstract

“…Similarly, for BSA, an apparent cmc of ∼0.076 μM has been reported in the literature, 22 with a constant equilibrium surface tension of 53-55 mN/m at higher concentrations. 38,47 Interfacial Tension of PFP against Aqueous Solutions. In the absence of any surfactants, the interfacial tension of PFP against pure distilled water was measured to be 54 dyn/cm, in excellent agreement with the literature value of 56 dyn/cm.…”

Section: Resultsmentioning

confidence: 99%

Oxygenation-Enhanced Radiation Therapy of Breast Tumors

Skliar¹

2011

View full text Add to dashboard Cite

Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. REPORT DATE (DD-MM-YYYY)2. REPORT TYPE 3. DATES COVERED (From -To) 4. TITLE AND SUBTITLE 5a. CONTRACT NUMBER 5b. GRANT NUMBER 5c. PROGRAM ELEMENT NUMBER 6. AUTHOR(S) 5d. PROJECT NUMBER 5e. TASK NUMBER E-Mail:5f. WORK UNIT NUMBER The treatment of locoregional breast cancer has evolved from radical mastectomy to targeted local therapy with breast conservation. The efficacy of conserving treatments of breast cancers is impeded by tumor hypoxia, which affects 50% of locally advanced breast tumors. Poor oxygenation of hypoxic tumors reduces their sensitivity to X-ray and γ-radiation, which requires a high radiation dose for efficacy compared to normally oxygenated tissues. This Concept project provides initial investigation the method for targeted oxygen release from oxygen carriers as a step towards as a novel strategy of radio sensitization of hypoxic breast tumors, and studies the effect of different targeting mechanisms on the oxygen mass transfer. Specific results include the development of stabilized perfluorocarbon emulsions as oxygen carriers, their characterization, and response to external triggers, including elevated temperature, reduced pressure, and dwell time. PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES) 8. PERFORMING ORGANIZATION REPORT NUMBER SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S) U.S. Army Medical Research and Materiel Command Fort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S) DISTRIBUTION / AVAILABILITY STATEMENT IntroductionThe treatment of locoregional breast cancer has evolved from radical mastectomy to targeted local therapy with breast conservation. The efficacy of conserving treatments of breast cancers is impeded by tumor hypoxia. It has been reported [1] that close to 50% of locally advanced breast cancers exhibit hypoxic or even anoxic regions within a tumor mass. Poor oxygenation of hypoxic tumors reduces their sensitivity to X-ray and γ-radiation, which requires a high radiation dose for efficacy compared to normally oxygenated tissues [2]. This increase is approximately 3-fold in the case of X-ray therapy [3], which ...

show abstract

Effect of concentration and denaturation on adsorption and surface tension of bovine serum albumin

Cited by 133 publications

References 26 publications

Protein Nanopatterning on Self-Organized Poly(styrene-b-isoprene) Thin Film Templates

Protein Nanopatterning on Self-Organized Poly(styrene-b-isoprene) Thin Film Templates

The adsorption and unfolding kinetics determines the folding state of proteins at the air–water interface and thereby the equation of state

Oxygenation-Enhanced Radiation Therapy of Breast Tumors

Contact Info

Product

Resources

About