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Objectives
Importance Composition & Models Important properties Specialized structures RBC membrane Biomembranes Transport mechanisms
Maintenance of shape Control of movement of molecules across Cell-cell recognition and communication Cellular movement
Chemical composition
Lipids
Phosphatidylcholine (lecithin) : 40-50% Sphingomyelins Glycolipids: 2-10% absent in prokaryotes Most rigid lipid in membrane
Sphingolipids:
Proteins
Glycoproteins
Membrane proteins
Enzymatic activity:
Carrier proteins:
Signal transduction:
Regulation of permeability
Membrane proteins
Peripheral proteins
Integral proteins
Embedded deeply (transmembrane) by hydrophobic bonds/ van der Waals force Removal requires use of detergents or organic solvents Transport proteins Removal causes denaturation of protein and loss of function
Amphipathic molecules Polar heads point outside, Non-polar tails point inwards Non-polar core acts as diffusion barrier: impermeable to polar molecules and ions 1925, Gorter and Grendel proposed lipid bilayer model 1935, Davson and Danielle suggested phospholipids as major constituent
1972, Singer and Nicholson Intrinsic proteins immersed in protein bilayer (60-100A) Extrinsic proteins loosely attached to surface of membrane Charecteristics:
Icebergs
Membrane asymmetry
Proteins are inserted in asymmetric fashion Oligosaccharide units project towards exterior Lipids are distributed asymmetrically:
Outer
leaflet:
Phosphatidylcholine Sphingolipids
Inner
leaflet:
Phosphatidylethanolamine
Phosphatidylserine
Membrane fluidity
Composition
Short
chain FA fluidity Cis- Unsaturated FA fluidity (more the no. of double bonds, the Tm)
RBC membrane
Glycophorin
Integral
Anion exchanger
Integral
Ankyrin
Peripheral
Other Biomembranes
Clinically
carriers
useful
Aquasomes
Most recently developed delivery system Used for proteins and peptides Structure: nanoparticulate, three layered, self assembled Central solid nanocrystalline core coated with polyhydroxy oligomers Biochemically active molecules adsorbed to this core Core gives structural stability and stabilizes active biological molecules Used for: Insulin, Hemoglobin, Antigens, Serratiopeptidase
Non lipid-soluble molecules are handled by membrane proteins: Channels for ions/ small mols Transporters for larger mols
Membrane phospholipids are solvents for membrane proteins - helical structures in proteins minimize hydrophilic character of peptide bonds Proteins are amphipathic Hydropathy plot
Lipid rafts
Exoplasmic
Caveolae
Caveolin-1
Tight junctions
Prevent
diffusion of macromolecules Located below apical surfaces, between cells Proteins: occludin, claudins
Transport processes
Passive diffusion
Gases: Highly permeable Water: Moderately permeable Ions and large polar molecules: Impermeable
Carrier-mediated transport
Porters/ translocases
Facilitated diffusion
Along concentration gradient, no energy consumed Transport protein hastens the process Mechanism:
oscillation
between two conformations: ping-pong Process is reversible Kinetics follow Michelis - Menten rate law
Egs.
Glucose
transporters: GLUT Chloride transporters: Cl- / HCO3- antiport and cystic fibrosis transmembrane conductance
Rate kinetics
Active transport
Solute moves against concentration gradient Expenditure of energy Primary active transport:
Energy
molecule moves coupled to another ion down its concentration gradient: Na- glucose symport No ATP hydrolysis, energy derived from electrochemical gradient of the primary ion
Ion channels
Transmembrane proteins Selective to certain ions Allow ionic transport at high rates Regulated Types:
Voltage
Affected by drugs
Aquaporins
Small cyclic organic molecules Shuttles for ions Eg. Valinomycin and Gramicidin, used as antibiotics
Tetrameric transmembrane proteins Permit passage of water only Mutations cause nephrogenic diabetes insipidus
Endocytosis
Exocytosis
Segments of plasma membrane invaginate and enclose small vol of ECF Phagocytosis and pinocytosis Primary and secondary lysosomes LDL mol and receptor internalized