Formation of amyloid β (Aβ) is a complex kinetic and thermodynamic process, dependent on peptide-peptide interactions that may be modulated by other proteins. We found that site-directed antibodies toward peptide (glutamic acid, phenyl alanine, arginine, histidine) EFRH sequences 3–6 of the N-terminal region of beta-amyloid peptide (AβP) suppress in vitro formation of Aβ and dissolve already formed fibrillar amyloid. These so-called chaperone-like properties of monoclonal antibodies led to the development of a new immunological approach toward Alzheimer’s disease (AD) treatment. Production and performance of anti-Aβ antibodies into the transgenic mouse model of AD showed that these antibodies may be delivered from the periphery to the central nervous system, preventing the formation of Aβ and dissolving amyloid plaques. Moreover, immunization with Aβ protects transgenic mice from the learning and age-related memory deficits that occur in AD. These data support the hypotheses that AβP plays a central role in AD, and site-directed antibodies that modulate AβP conformation might lead toward immunotherapy of the disease.