Producing the Controlled Hybrid lattice of Natural Protein Nanotubes by Chemical Hydrolysis for Nanomedicine Pegah Esmaeilzadeh 1a , Zahra Fakhroueian* 2b , Pouriya Esmaeilzadeh 3c 1 Martin Luther University Halle-Wittenberg, Institute of Pharmacy, Biomedical MaterialDepartment, Germany. 2 Institute of Petroleum Engineering, P.O.Box:11155-4563, University of Tehran, Iran. 3 Process simulation and control Lab. chemical Engineering collage, Iran University of Science and Technology (IUST), Narmak, Tehran, Iran. a pegah.esmaeilzadeh@pharmazie.uni-halle.de b , fakhroueian@ut.ac.ir (corresponding author), c pouriya66@yahoo.com Keywords: Nanobiotechnology, Protein Nanohybrids, Protein Nanotubes, Sol-Gel Method, Nanomedicine, Protein hybrid lattice, Nanotubes-Nanorods Hybrids. Abstract. This work was instigated by the fact that sol-gel chemistry provides a relatively simple way to incorporate recognition species in a stable host green environment. In this new strategy, which represents a low cost example of bottom-up nano-assembly, chemistry art is entering the field of nanobiotechnology in fabrication and control of an expanded homogeneous length of separate single-walled and ordered, helical lattice-like open-ended natural protein nanotubes(PNTs) and also creative novel bio-nanohybrids. A new type of protein nanohybrids containg nanotubes- nanorods, nanotubes-nanofibers, nanotubes core-shell nanofibers were prepared using an electrostatic self-assembly method with the aid of chemical partial hydrolysis of milk protein α- lactalbumin (sol-gel technique) at a suitable pH value for the first time. They can have long helically coiled length and are promising for high capacity drug loading and applying in nanomedicine as organ transplantation in human body and implant material, because of their improved stability and unique mechanical and lattice thermal resistivity properties. In this study, various valuable ligand or binding sites such as distinct Mn +2 , Ca +2 or Zn +2 cations were used for incorporated into protein nanostructures as the self-assembly essential stimulant motor. It was found that the designed nanobioproducts could retain and stabilize as very clear and transparent green aqueous nanobiofluids during two years. Introduction Over recent years of advancement in nanoparticles, drug delivery is widely expected to change the landscape of pharmaceutical and nano-biotechnology industries for the foreseeable future. A typical nanohybrid has emerged as a promising strategy for the efficient delivery of drugs used in the treatment of cancer by avoiding the reticuloendothelial system, utilizing the enhanced permeability and retention effect and tumor-specific targeting. Carbon nanofibers and functionalized multiwalled carbon nanotubes (CNT) are found to be an effective strategy for building a biosensor platform [1, 2]. Recently, nanohybrids, quantum dots and CNTs have been proposed as significant drug delivery carriers [3]. Nanohybrids combine biological or bio-functionalized molecules giving rise to a system capable of drug delivery with an emphasis toward cancer therapy. Natural protein nanotubes (PNTs) containing lattice nanohybrids are hydrophilic character in nature and thus soluble in water, which do not limit their application in biomedical and medicinal chemistry so as to avoid their aggregation and to facilitate their use in clinical applications. This work was instigated by the fact that nonhydrolytic sol-gel chemistry provides a relatively simple way to incorporate recognition species in a stable host environment [4]. In this new strategy which represent a low cost example of bottom-up assembly, chemistry is entering the field of nanoscale science, which was originally physics-oriented. This novel well-orchestrated mechanism offer obvious advantages as a ‘smart’ nanoparticles-based system. The types of smartness that have Journal of Nano Research Vol. 21 (2013) pp 7-13 © (2013) Trans Tech Publications, Switzerland doi:10.4028/www.scientific.net/JNanoR.21.7 All rights reserved. No part of contents of this paper may be reproduced or transmitted in any form or by any means without the written permission of TTP, www.ttp.net. (ID: 81.201.144.193-13/12/12,18:43:50)