IGEM:IMPERIAL/2008/Prototype/Biomaterials

From OpenWetWare
Jump to navigationJump to search

<html> <style type="text/css"> .firstHeading {display: none;} </style> </html> <html> <style type="text/css">

   table.calendar          { margin:0; padding:2px; }

table.calendar td { margin:0; padding:1px; vertical-align:top; } table.month .heading td { padding:1px; background-color:#FFFFFF; text-align:center; font-size:120%; font-weight:bold; } table.month .dow td { text-align:center; font-size:110%; } table.month td.today { background-color:#3366FF } table.month td {

   border:2px;
   margin:0;
   padding:0pt 1.5pt;
   font-size:8pt;
   text-align:right;
   background-color:#FFFFFF;
   }
  1. bodyContent table.month a { background:none; padding:0 }

.day-active { font-weight:bold; } .day-empty { color:black; } </style> </html>

<html><script language="JavaScript">

var timeout = 250; var closetimer = 0; var ddmenuitem = 0;

// open hidden layer function mopen(id) { // cancel close timer mcancelclosetime(); // close old layer if(ddmenuitem) ddmenuitem.style.visibility = 'hidden'; // get new layer and show it ddmenuitem = document.getElementById(id); ddmenuitem.style.visibility = 'visible'; } // close showed layer function mclose() { if(ddmenuitem) ddmenuitem.style.visibility = 'hidden'; } // go close timer function mclosetime() { closetimer = window.setTimeout(mclose, timeout); } // cancel close timer function mcancelclosetime() { if(closetimer) { window.clearTimeout(closetimer); closetimer = null; } } // close layer when click-out //document.onclick = mclose; </script>




</html>
<html><style type="text/css">

div.Section { font:11pt/16pt Calibri, Verdana, Arial, Geneva, sans-serif; background-image: url(http://openwetware.org/images/a/a0/Background.PNG); background-size: 100%; background-origin: content; }

/* Text (paragraphs) */ div.Section p { font:11pt/16pt Calibri, Verdana, Arial, Geneva, sans-serif; text-align:justify; margin-top:0px; margin-left:30px; margin-right:30px; }

/* Headings */ div.Section h1 { font:22pt Calibri, Verdana, Arial, Geneva, sans-serif; text-align:left; color:#3366FF; font-weight:bold; }

/* Subheadings */ div.Section h2 { font:18pt Calibri, Verdana, Arial, Geneva, sans-serif; color:#3366FF; margin-left:5px; font-weight:bold; }

/* Subsubheadings */ div.Section h3 { font:22pt Calibri, Verdana, Arial, sans-serif; color:#E5EBFF; margin-left:10px; font-weight:bold; }

/* Subsubsubheadings */ div.Section h4 { font:22pt Calibri, Verdana, Arial, sans-serif; color:#2B48B3; margin-left:10px; font-weight:bold; }

/* Subsubsubsubheadings */ div.Section h5 { font:12pt Calibri, Verdana, Arial, sans-serif; color:#3366FF; margin-left:20px; }

/* References */ div.Section h6 { font:12pt Calibri, Verdana, Arial, sans-serif; font-weight:bold; font-style:italic; color:#3366FF; margin-left:25px; }

/* Hyperlinks */ div.Section a { }

div.Section a:hover { }

/* Tables */ div.Section td { font:11pt/16pt Calibri, Verdana, Arial, Geneva, sans-serif; text-align:justify; vertical-align:top; padding:2px 4px 2px 4px; }

/* Lists */ div.Section li { font:11pt/16pt Calibri, Verdana, Arial, Geneva, sans-serif; text-align:left; margin-top:0px; margin-left:30px; margin-right:0px; }

/* TOC stuff */ table.toc { margin-left:10px; }

table.toc li { font: 11pt/16pt Calibri, Verdana, Arial, Geneva, sans-serif; text-align: justify; margin-top: 0px; margin-left:2px; margin-right:2px; }

/* [edit] links */ span.editsection { color:#BBBBBB; font-size:10pt; font-weight:normal; font-style:normal; vertical-align:bottom; }

span.editsection a { color:#BBBBBB; font-size:10pt; font-weight:normal; font-style:normal; vertical-align:bottom; }

span.editsection a:hover { color:#3366FF; font-size:10pt; font-weight:normal; font-style:normal; vertical-align:bottom; }

/* Drop-down Menu */

  1. sddm {

margin: 0; padding: 0; z-index: 30 margin: 0; padding: 0; float: center; font: bold 12pt Calibri, Verdana, Arial, Geneva, sans-serif; border: 0px; list-style: none; }

  1. sddm a {

display: block; margin: 0px 0px 0px 0px; padding: 0 0 12px 0; color: #FFFFFF; text-align: center; text-decoration: none; }

  1. sddm a:hover {

border: 0px }

  1. sddm div {

position: absolute; visibility: hidden; margin: 0; padding: 0; background: #66aadd; border: 1px solid #66aadd } #sddm div a { position: relative; left: 0; display: block; margin: 0; padding: 5px 10px; width: auto; white-space: nowrap; text-align: left; text-decoration: none; background: #FFFFFF; color: #2875DE; font: 11pt Calibri, Verdana, Arial, Geneva, sans-serif } #sddm div a:hover { background: #66aadd; color: #FFFFFF } </style></html>


Biomaterials

We aim to synthesize two types of biomaterials, elastin and EAK16-II 3D scaffolds.


Elastin

Elastin is a polymeric extracellular matrix protein found in tissues that require the abitlity to extend as well as posses elastic recoil. Examples of elastin containing tissues include arteries, lungs, ligaments and skin. The precursor for elastin is a soluble protein called tropoelastin, consisting of alternating hydrophobic regions and crosslinking domains with distinct exons coding each domain.

Under appropriate conditions of temperature and ionic strength, elastin undergoes a self-aggregation process called coacervation. This is where the protein separates from the solution as a second phase and is usually induced by an increase in temperature.

Unlike most proteins, which undergo denaturation when the temperature of the solution increases, elastin polypeptides become more ordered through coacervation. The temperature at which coacervation occurs is dependent on the relative proportions of hydrophobic and hydrophilic residues in the synthetic polypeptides as well as the ionic strength, pH and protein concentration of the solution.

Error creating thumbnail: File missing

Error creating thumbnail: File missing

Error creating thumbnail: File missing


EAK16-II

EAK16-II is a self-assembling peptide which forms stable β-sheet structures in water and exists naturally as a region in zuotin, a yeast protein. The amino acid sequence for EAK16-II is AEAEAKAKAEAEAKAK and has an estimated molecular mass of 1615.8. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II proteins and these nanofibres can futher aggregate to form a membranous 3D scaffold.

The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides and self-assembly is triggered when the proteins are exposed to physiological media or salt solution.

Error creating thumbnail: File missing


How B. subtilis can be used in producing material



References
Error fetching PMID 11738083
Error fetching PMID 11911775
Error fetching PMID 16061392
Error fetching PMID 16997527
Error fetching PMID 10974125
  1. Error fetching PMID 11738083 [Elastin]
  2. Error fetching PMID 11911775 [Elastin]
  3. Error fetching PMID 16061392 [EAK16-II]
  4. Error fetching PMID 16997527 [ProteinSecretion]
  5. Error fetching PMID 10974125 [Proteomics]
All Medline abstracts: PubMed | HubMed