Molecular Playground/Human Serum Albumin

2014-12-03T23:13:47Z

Mahalia Serrano:

== '''HUMAN SERUM ALBUMIN (HSA)''' ==

<Structure load='4iw1' size='500' frame='true' align='right' caption='Human serum albumin (PDB code [[4iw1]])' scene='Insert optional scene name here' />

'''Human serum albumin''' (HSA) is the most abundant protein in the blood plasma, amounting to about 35 to 50 grams per liter of serum. With a molecular weight of about 66.5 kDa, it consists mostly of <scene name='57/571397/Alpha_helices/1'>alpha helices</scene> that form several hydrophobic binding pockets throughout the molecule.

== Structure ==

<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>

Being the major protein in blood, it functions to maintain the osmotic pressure and the pH of the blood. But most importantly, it functions to transport various substances through the bloodstream. HSA does not carry a specific cargo, although it does have preference for fat-soluble substances as it can bury the water-insoluble molecules into its hydrophobic core. Here, we can see <scene name='57/571397/Hsa_with_myr_and_aspirin/5'>HSA with both myristate (a fatty acid, shown in grey spheres) and aspirin (a common analgesic, shown in pink) bound</scene> to its hydrophobic pockets. HSA transports a wide variety of substances through the bloodstream including carbohydrates (e.g <scene name='57/571397/Hsa_with_glucose/6'>glucose</scene>), fatty acids (e.g. <scene name='57/571397/Hsa_with_arachidonic_acid/3'>arachidonic acid</scene>), hormones (e.g. <scene name='57/571397/Hsa_with_thyroxine/6'>thyroxine</scene>, a thyroid hormone), and drugs (e.g. <scene name='57/571397/Hsa_with_ibp/1'>ibuprofen</scene>, an anti-inflammatory drug).

Because HSA is very abundant in blood serum, most biomarker studies involving serum requires preliminary removal of HSA so that other non-abundant but otherwise important disease-indicating proteins can be detected. In our group, we exploit several properties of HSA in order to efficiently remove it from serum prior to biomarker analysis. These properties include its low isoelectric point (pI of about 4.7) due to a number of <scene name='57/571397/Overall_structure_of_hsa/5'>acidic residues</scene>, and its tendency to bind hydrophobic molecules through its hydrophobic pockets.

Molecular Playground/Human Serum Albumin

2014-12-03T22:53:25Z

2014-12-03T17:28:52Z

Mahalia Serrano:

Molecular Playground/Human Serum Albumin

2014-12-03T17:27:59Z

Mahalia Serrano:

== '''HUMAN SERUM ALBUMIN (HSA)''' ==
<Structure load='4k2c' size='500' frame='true' align='right' caption='Human serum albumin dimer (PDB code [[4k2c]])' scene='Insert optional scene name here' />
<scene name='57/571397/Start/3'>TextToBeDisplayed</scene>
'''Human serum albumin''' (HSA) is the most abundant protein in the blood plasma, amounting to about 35 to 50 grams per liter of serum. It consists mostly of <scene name='57/571397/Overall_structure_of_hsa/3'>alpha helices</scene> that form several hydrophobic binding pockets throughout the molecule.

Being the major protein in blood, it functions to maintain the osmotic pressure and the pH of the blood. But most importantly, it functions to transport various substances through the bloodstream. HSA does not carry a specific cargo, although it does have preference for fat-soluble substances as it can bury the water-insoluble molecules into its hydrophobic core. Here, we can see <scene name='57/571397/Hsa_with_myr_and_aspirin/5'>HSA with both myristate (a fatty acid, shown in grey spheres) and aspirin (a common analgesic, shown in pink) bound</scene> to its hydrophobic pockets. HSA transports a wide variety of substances through the bloodstream including carbohydrates (e.g <scene name='57/571397/Hsa_with_glucose/6'>glucose</scene>), fatty acids (e.g. <scene name='57/571397/Hsa_with_arachidonic_acid/3'>arachidonic acid</scene>), hormones (e.g. <scene name='57/571397/Hsa_with_thyroxine/6'>thyroxine</scene>, a thyroid hormone), and drugs (e.g. <scene name='57/571397/Hsa_with_ibp/1'>ibuprofen</scene>, an anti-inflammatory drug).

Because HSA is very abundant in blood serum, most biomarker studies involving serum requires preliminary removal of HSA so that other non-abundant but otherwise important disease-indicating proteins can be detected. In our group, we exploit several properties of HSA in order to efficiently remove it from serum prior to biomarker analysis. These properties include its low isoelectric point (pI of about 4.7) due to a number of <scene name='57/571397/Overall_structure_of_hsa/5'>acidic residues</scene>, and its tendency to bind hydrophobic molecules through its hydrophobic pockets.