Spectroscopic Microscopy Analysis of the Interior pH of Individual Phospholipid Vesicles

2011 ◽  
Vol 83 (21) ◽  
pp. 8230-8238 ◽  
Author(s):  
Emily C. Heider ◽  
Grant A. Myers ◽  
Joel M. Harris
Keyword(s):  
Phospholipid Vesicles ◽  
Individual Phospholipid ◽  
Microscopy Analysis

Detection of Drug−Membrane Interactions in Individual Phospholipid Vesicles by Confocal Raman Microscopy

2006 ◽  
Vol 78 (14) ◽  
pp. 4918-4924 ◽  
Author(s):  
Christopher B. Fox ◽  
Robert A. Horton ◽  
Joel M. Harris
Keyword(s):  
Raman Microscopy ◽  
Phospholipid Vesicles ◽  
Individual Phospholipid ◽  
Confocal Raman Microscopy ◽  
Membrane Interactions ◽  
Confocal Raman

Material analysis techniques using the ion mill

1996 ◽  
Vol 54 ◽  
pp. 1034-1035
Author(s):  
J. P. Benedict ◽  
R. M. Anderson ◽  
S. J. Klepeis
Keyword(s):  
Polished Surface ◽  
Surface Material ◽  
Analysis Techniques ◽  
Material Analysis ◽  
Optical Inspection ◽  
Electron Microscopy Analysis ◽  
Microscopy Analysis ◽  
Argon Ions ◽  
The Impact ◽  
Scanning Electron

Ion mills equipped with flood guns can perform two important functions in material analysis; they can either remove material or deposit material. The ion mill holder shown in Fig. 1 is used to remove material from the polished surface of a sample for further optical inspection or SEM ( Scanning Electron Microscopy ) analysis. The sample is attached to a pohshing stud type SEM mount and placed in the ion mill holder with the polished surface of the sample pointing straight up, as shown in Fig 2. As the holder is rotating in the ion mill, Argon ions from the flood gun are directed down at the top of the sample. The impact of Argon ions against the surface of the sample causes some of the surface material to leave the sample at a material dependent, nonuniform rate. As a result, the polished surface will begin to develop topography during milling as fast sputtering materials leave behind depressions in the polished surface.

A heteronuclear and homonuclear filtering strategy for studying the structure of membrane peptides in non-deuterated phospholipid vesicles

1998 ◽  
Vol 95 (2) ◽  
pp. 221-224
Author(s):  
B. T. Doan ◽  
C. Nezry ◽  
L. Rene ◽  
B. Badet ◽  
J. C. Beloeil
Keyword(s):  
Phospholipid Vesicles ◽  
Membrane Peptides

Thermally induced budding of phospholipid vesicles — a discontinuous process

1993 ◽  
Vol 3 (5) ◽  
pp. 631-645 ◽  
Author(s):  
J. Käs ◽  
E. Sackmann ◽  
R. Podgornik ◽  
S. Svetina ◽  
B. Žekš
Keyword(s):  
Phospholipid Vesicles ◽  
Thermally Induced ◽  
Discontinuous Process

Plasma Factor V Activation Is Prevented by Activated Protein C in the Presence of Phospholipid Vesicles, Not Platelets

1993 ◽  
Vol 69 (02) ◽  
pp. 124-129 ◽  
Author(s):  
Susan Solymoss ◽  
Kim Thi Phu Nguyen
Keyword(s):  
Western Blotting ◽  
Protein C ◽  
Thrombin Generation ◽  
Blood Platelets ◽  
Activated Protein C ◽  
Phospholipid Vesicles ◽  
Factor V ◽  
Two Stage ◽  
One Stage ◽  
Plasma Factor

SummaryActivated protein C (APC) is a vitamin K dependent anticoagulant which catalyzes the inactivation of factor Va and VIIIa, in a reaction modulated by phospholipid membrane surface, or blood platelets. APC prevents thrombin generation at a much lower concentration when added to recalcified plasma and phospholipid vesicles, than recalcified plasma and platelets. This observation was attributed to a platelet associated APC inhibitor. We have performed serial thrombin, factor V one stage and two stage assays and Western blotting of dilute recalcified plasma containing either phospholipid vesicles or platelets and APC. More thrombin was formed at a given APC concentration with platelets than phospholipid. One stage factor V values increased to higher levels with platelets and APC than phospholipid and APC. Two stage factor V values decreased substantially with platelets and 5 nM APC but remained unchanged with phospholipid and 5 nM APC. Western blotting of plasma factor V confirmed factor V activation in the presence of platelets and APC, but lack of factor V activation with phospholipid and APC. Inclusion of platelets or platelet membrane with phospholipid enhanced rather than inhibited APC catalyzed plasma factor V inactivation. Platelet activation further enhanced factor V activation and inactivation at any given APC concentration.Plasma thrombin generation in the presence of platelets and APC is related to ongoing factor V activation. No inhibition of APC inactivation of FVa occurs in the presence of platelets.

Glycoproteins IIb and IIIa and Platelet Thrombospondin in a Liposome Model of Platelet Aggregation

1986 ◽  
Vol 55 (02) ◽  
pp. 240-245 ◽  
Author(s):  
M E Rybak
Keyword(s):  
Platelet Aggregation ◽  
Direct Evidence ◽  
Phospholipid Vesicles ◽  
Aggregate Formation ◽  
Membrane Glycoproteins ◽  
Protein Orientation ◽  
Phosphatidylcholine Liposomes ◽  
Calcium Dependent ◽  
Lentil Lectin ◽  
Complete Reversal

SummaryPlatelet membrane glycoproteins IIb and IIIa and platelet thrombospondin were incorporated onto phosphatidylcholine liposomes, by freeze thawing and sonication. Protein orientation on the liposomes was confirmed by susceptibility to neuraminidase cleavage and binding to lentil lectin-Sepharose (GPIIb-IIIa liposomes) and to heparin-Sepharose (thrombospondin liposomes). Glycoproteins Ilb-IIIa bound 125I-fibrinogen with Kd of 7.5 × 10™7M. Binding was reversible and calcium-dependent. Ilb-IIIa liposomes underwent fibrinogen-dependent aggregation in the presence of 10 mM CaCl2. Maximal aggregate formation was observed with a combination of IIb-IIIa liposomes and thrombospondin liposomes. This aggregation was partially inhibited by preincubation with monoclonal antibodies to the IIb-IIIa complex. Addition of EDTA caused complete reversal of aggregates. Thrombospondin liposomes also underwent fibrinogen and calcium dependent aggregation, however, this aggregation was less than that observed with the GPIIb-IIIa liposomes. Maximal aggregate formation was observed with a mixture of IIb-IIIa liposomes and thrombospondin liposomes. These studies demonstrate that GPIIb-IIIa and thrombospondin can be incorporated into phospholipid vesicles with preservation of function. Direct evidence is provided to demonstrate that glycoprotein lib and Ilia and fibrinogen are sufficient for platelet aggregation and to demonstrate that thrombospondin may also contribute to platelet aggregation.

Properties of Stabilized Sub-Micron Phospholipid Vesicles.

1987 ◽  
Author(s):  
John D. Baldeschwieler
Keyword(s):  
Phospholipid Vesicles

TUNING PROPERTIES AND MORPHOLOGY IN HIGH VINYL CONTENT SBS BLOCK COPOLYMER, A THERMOPLASTIC ELASTOMER VIA THIOL-ENE MODIFICATION

2017 ◽  
Vol 90 (3) ◽  
pp. 550-561 ◽  
Author(s):  
Prithwiraj Mandal ◽  
Siva Ponnupandian ◽  
Soumyadip Choudhury ◽  
Nikhil K. Singha
Keyword(s):  
Block Copolymer ◽  
Thermoplastic Elastomer ◽  
Atomic Force Microscopy Analysis ◽  
Ene Reaction ◽  
Force Microscopy ◽  
Atomic Force ◽  
Microscopy Analysis ◽  
Styrene Butadiene Styrene ◽  
Styrene Butadiene ◽  
Butadiene Styrene

ABSTRACT Thiol-ene modification of high vinyl content thermoplastic elastomeric styrene butadiene styrene (SBS) block copolymer (BCP) was carried out using different thiolating agents in toluene at 70 °C. 1H NMR analysis confirmed the participation of vinyl double bond in the thiol-ene modification reaction of SBS. Surface morphology of the block copolymers evaluated by atomic force microscopy analysis showed higher roughness after the thiol-ene reaction. The thiol-modified SBS block copolymer showed better adhesion strength and oil resistance properties than the pristine SBS.

scholarly journals Atomic force microscopy analysis of native infectious and inactivated SARS-CoV-2 virions

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sébastien Lyonnais ◽  
Mathilde Hénaut ◽  
Aymeric Neyret ◽  
Peggy Merida ◽  
Chantal Cazevieille ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Native Conformation ◽  
Force Microscopy ◽  
Enveloped Virus ◽  
Atomic Force ◽  
Afm Imaging ◽  
Level 3 ◽  
Microscopy Analysis ◽  
Virus Morphology ◽  
Nanoscale Level

AbstractSARS-CoV-2 is an enveloped virus responsible for the Coronavirus Disease 2019 (COVID-19) pandemic. Here, single viruses were analyzed by atomic force microscopy (AFM) operating directly in a level 3 biosafety (BSL3) facility, which appeared as a fast and powerful method to assess at the nanoscale level and in 3D infectious virus morphology in its native conformation, or upon inactivation treatments. AFM imaging reveals structurally intact infectious and inactivated SARS-CoV-2 upon low concentration of formaldehyde treatment. This protocol combining AFM and plaque assays allows the preparation of intact inactivated SARS-CoV-2 particles for safe use of samples out of level 3 laboratory to accelerate researches against the COVID-19 pandemic. Overall, we illustrate how adapted BSL3-AFM is a remarkable toolbox for rapid and direct virus analysis based on nanoscale morphology.

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