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Phosphoinositides and PIPs

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

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PNIPAM Mesoglobules in Dependence on Pressure.

Bart-Jan Niebuur¹, Vitaliy Pipich², Marie-Sousai Appavou²

¹TUM School of Natural Sciences, Physics Department, Soft Matter Physics Group, Technical University of Munich, James-Franck-Str. 1, Garching 85748, Germany.

Langmuir : the ACS Journal of Surfaces and Colloids

|October 12, 2024

Summary

Poly(N-isopropylacrylamide) (PNIPAM) forms mesoglobules in water. High pressure causes these mesoglobules to swell, with a transition dependent on temperature and pressure, revealing distinct low- and high-pressure regimes.

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Area of Science:

Polymer Science
Physical Chemistry
Soft Matter Physics

Background:

Poly(N-isopropylacrylamide) (PNIPAM) exhibits a lower critical solution temperature (LCST) behavior in aqueous solutions.
Above its cloud point temperature (Tcp), PNIPAM forms mesoglobules, which change in size and water content with pressure.

Purpose of the Study:

To investigate the pressure-induced transition of PNIPAM mesoglobules.
To characterize the size and water content of mesoglobules under varying pressure and temperature conditions.
To identify the transition line separating low- and high-pressure regimes.

Main Methods:

Isothermal pressure scans using optical microscopy.
Very small angle neutron scattering (VSANS) to determine mesoglobule size and water content.
Analysis of mesoglobule behavior at different temperatures above Tcp.

Main Results:

A distinct transition in mesoglobule state occurs between 35-55 MPa, dependent on temperature.
The transition is smooth at high temperatures (far from coexistence) and abrupt at low temperatures (near coexistence).
At high temperatures, mesoglobule swelling dominates; at low temperatures, coalescence prevails, with incomplete disintegration of aggregates upon pressure decrease.

Conclusions:

A new transition line is identified, separating distinct low- and high-pressure regimes for PNIPAM mesoglobules.
The pressure-induced transition exhibits temperature-dependent characteristics, influencing mesoglobule swelling and coalescence.
Historical effects (cooling at high pressure) show limited impact on the observed transition, suggesting partial reversibility of mesoglobule aggregation.