Antimicrobial peptides - Revision history

Michal Harel at 08:59, 6 January 2019

Michal Harel — Sun, 06 Jan 2019 08:59:35 GMT

←Older revision		Revision as of 08:59, 6 January 2019
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	==Antimicrobial peptides==		==Antimicrobial peptides==
-	<StructureSection load='3rec' size='350' side='right' caption='' scene='67/676980/4mgp_ala-mag/1'>	+	<StructureSection load='3rec' size='350' side='right' caption='Magainin 2 peptide (PDB code [[4mgp]])' scene='67/676980/4mgp_ala-mag/1'>

Tal stern at 14:52, 1 February 2015

Tal stern — Sun, 01 Feb 2015 14:52:21 GMT

←Older revision		Revision as of 14:52, 1 February 2015
Line 145:		Line 145:

	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:Barrel stave pore model.JPG\|~~frameless~~\|~~350px~~]]	+	[[Image:Barrel stave pore model.JPG\|center\|400px]]


	'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
-	[[Image:Torodial pore model.JPG\|center\|~~350px~~]]	+	[[Image:Torodial pore model.JPG\|center\|400px]]

	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
Line 155:		Line 155:

	'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.		'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.
-	[[Image:Detergent model.JPG\|~~350px~~]]	+	[[Image:Detergent model.JPG\|center\|400px]]


	== Relevance ==		== Relevance ==

-		+	[[magainin 2]]

	</StructureSection>		</StructureSection>

Tal stern at 14:50, 1 February 2015

Tal stern — Sun, 01 Feb 2015 14:50:21 GMT

←Older revision		Revision as of 14:50, 1 February 2015
Line 145:		Line 145:

	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:Barrel stave pore model.JPG\|~~frame~~\|350px]]	+	[[Image:Barrel stave pore model.JPG\|frameless\|350px]]


	'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
-	[[Image:Torodial pore model.JPG\|~~thumb~~\|350px]]	+	[[Image:Torodial pore model.JPG\|center\|350px]]

	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
Line 155:		Line 155:

	'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.		'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.
-	[[Image:Detergent model.JPG~~\|right~~\|350px]]	+	[[Image:Detergent model.JPG\|350px]]

Tal stern at 14:48, 1 February 2015

Tal stern — Sun, 01 Feb 2015 14:48:57 GMT

←Older revision		Revision as of 14:48, 1 February 2015
Line 145:		Line 145:

	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:Barrel stave pore model.JPG\|~~right~~\|350px]]	+	[[Image:Barrel stave pore model.JPG\|frame\|350px]]


	'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
-	[[Image:Torodial pore model.JPG\|~~right~~\|350px]]	+	[[Image:Torodial pore model.JPG\|thumb\|350px]]

	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:

Tal stern at 14:47, 1 February 2015

Tal stern — Sun, 01 Feb 2015 14:47:15 GMT

←Older revision		Revision as of 14:47, 1 February 2015
Line 145:		Line 145:

	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:Barrel stave pore model.JPG\|right\|~~200px~~]]	+	[[Image:Barrel stave pore model.JPG\|right\|350px]]


	'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
-	[[Image:Torodial pore model.JPG]]	+	[[Image:Torodial pore model.JPG\|right\|350px]]

	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
Line 155:		Line 155:

	'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.		'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.
-	[[Image:Detergent model.JPG]]	+	[[Image:Detergent model.JPG\|right\|350px]]

Tal stern at 14:46, 1 February 2015

Tal stern — Sun, 01 Feb 2015 14:46:03 GMT

←Older revision		Revision as of 14:46, 1 February 2015
Line 145:		Line 145:

	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:Barrel stave pore model.JPG]]	+	[[Image:Barrel stave pore model.JPG\|right\|200px]]

Tal stern at 22:00, 31 January 2015

Tal stern — Sat, 31 Jan 2015 22:00:33 GMT

←Older revision		Revision as of 22:00, 31 January 2015
Line 143:		Line 143:
	In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that it cannot hold it's content anymore.		In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that it cannot hold it's content anymore.
	The''' transmembrane pore mechanism''' has 2 main models:		The''' transmembrane pore mechanism''' has 2 main models:
		+
	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
	[[Image:Barrel stave pore model.JPG]]		[[Image:Barrel stave pore model.JPG]]
Line 152:		Line 153:
	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
	'''1- The carpet model''': In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.		'''1- The carpet model''': In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.
		+
	'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.		'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.
	[[Image:Detergent model.JPG]]		[[Image:Detergent model.JPG]]

Tal stern at 21:59, 31 January 2015

Tal stern — Sat, 31 Jan 2015 21:59:41 GMT

←Older revision		Revision as of 21:59, 31 January 2015
Line 142:		Line 142:

	In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that it cannot hold it's content anymore.		In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that it cannot hold it's content anymore.
-	~~tha~~ transmembrane pore mechanism has 2 main models:	+	The''' transmembrane pore mechanism''' has 2 main models:
-	1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.	+	'''1- barrel stave pore model''' ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
	[[Image:Barrel stave pore model.JPG]]		[[Image:Barrel stave pore model.JPG]]


-	2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..	+	'''2- toroidal pore model''', that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
	[[Image:Torodial pore model.JPG]]		[[Image:Torodial pore model.JPG]]

-	the Nonepore model claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:	+	the '''Nonepore model''' claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
-	1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.	+	'''1- The carpet model''': In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.
-	2- detergent model- collapse of membrane integrity, observed with some AMPs at high peptide concentration.	+	'''2- detergent model''' : collapse of membrane integrity, observed with some AMPs at high peptide concentration.
	[[Image:Detergent model.JPG]]		[[Image:Detergent model.JPG]]

Tal stern at 21:55, 31 January 2015

Tal stern — Sat, 31 Jan 2015 21:55:54 GMT

←Older revision		Revision as of 21:55, 31 January 2015
Line 145:		Line 145:
	1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
	[[Image:Barrel stave pore model.JPG]]		[[Image:Barrel stave pore model.JPG]]
		+

	2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..
-	[[Image:~~Torodial_pore_model~~.JPG]]	+	[[Image:Torodial pore model.JPG]]

	the Nonepore model claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:		the Nonepore model claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms:
	1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.		1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization.
	2- detergent model- collapse of membrane integrity, observed with some AMPs at high peptide concentration.		2- detergent model- collapse of membrane integrity, observed with some AMPs at high peptide concentration.
-	[[Image:~~Detregent_model~~.JPG]]	+	[[Image:Detergent model.JPG]]
-		+

Tal stern at 21:53, 31 January 2015

Tal stern — Sat, 31 Jan 2015 21:53:09 GMT

←Older revision		Revision as of 21:53, 31 January 2015
Line 144:		Line 144:
	tha transmembrane pore mechanism has 2 main models:		tha transmembrane pore mechanism has 2 main models:
	1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.		1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel.
-	[[Image:~~Barrel_stave_pore_model~~.JPG]]	+	[[Image:Barrel stave pore model.JPG]]

	2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..		2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure..