CAPTCHA AS GRAPHICAL PASSWORDS—A NEW SECURITY PRIMITIVE BASED ON HARD AI PROBLEMS

Many security primitives are based on hard mathematical problems. Using hard AI problems for security is emerging as an exciting new paradigm, but has been under-explored. In this paper, we present a new security primitive based on hard AI problems, namely, a novel family of graphical password systems built on top of Captcha technology, which we call Captcha as graphical passwords (CaRP). CaRP is both a Captcha and a graphical password scheme. CaRP addresses a number of security problems altogether, such as online guessing attacks, relay attacks, and, if combined with dual-view technologies, shoulder-surfing attacks. Notably, a CaRP password can be found only probabilistically by automatic online guessing attacks even if the password is in the search set. CaRP also offers a novel approach to address the well-known image hotspot problem in popular graphical password systems, such as PassPoints, that often leads to weak password choices. CaRP is not a panacea, but it offers reasonable security and usability and appears to fit well with some practical applications for improving online security

A Biologically Active Surface Enzyme Assembly that Attenuates Thrombus Formation

Activation of hemostatic pathways by blood‐contacting materials remains a major hurdle in the development of clinically durable artificial organs and implantable devices. Here, it is postulated that surface‐induced thrombosis may be attenuated by the reconstitution onto blood contacting surfaces of bioactive enzymes that regulate the production of thrombin, a central mediator of both coagulation and platelet activation cascades. Thrombomodulin (TM), a transmembrane protein expressed by endothelial cells, is an established negative regulator of thrombin generation in the circulatory system. Traditional techniques to covalently immobilize enzymes on solid supports may modify residues contained within or near the catalytic site, thus reducing the bioactivity of surface enzyme assemblies. In this report, a molecular engineering and bioorthogonal chemistry approach to site‐specifically immobilize a biologically active recombinant human TM fragment onto the luminal surface of small diameter prosthetic vascular grafts is presented. Bioactivity and biostability of TM modified grafts is confirmed in vitro and the capacity of modified grafts to reduce platelet activation is demonstrated using a non‐human primate model. These studies indicate that molecularly engineered interfaces that display TM actively limit surface‐induced thrombus formation. A biologically active thrombomodulin surface assembly to limit interfacial thrombin production was generated on the lumen of clinical ePTFE vascular grafts by site‐specific covalent immobilization. Therapeutic capacity of this biomimetic surface engineering approach to attenuate thrombus formation was demonstrated in a clinically relevant in vivo model of prosthetic graft thrombosis.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/89494/1/4736_ftp.pd